GenScript

His Tag Monoclonal Antibody (6G2A9), HRP, THE™

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His Tag Antibody (A00612) in WB

Western blot analysis of His-tagged protein using THE™ His Tag Antibody [HRP], mAb, Mouse (A00612, 1 µg/mL)The signal was developed with LumiSensor TM HRP Substrate Kit (GenScript, L00221).

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Product Details

A00612

Applications

Tested Dilution

Publications

Western Blot (WB)

0.1-1.0 µg/mL

ELISA (ELISA)

0.05-0.5 µg/mL

Miscellaneous PubMed (MISC)

View 8 publications 8 publications

Product Specifications

Species Reactivity

Tag

Host/Isotype

Mouse / IgG1, kappa

Class

Monoclonal

Type

Antibody

Clone

6G2A9

Immunogen

A synthetic peptide HHHHHH coupled to KLH

Conjugate

HRP HRP HRP

Form

Lyophilized

Purification

Protein A

Storage buffer

PBS, pH 7.4, with 1% BSA

Contains

0.01% thimerosal

Storage conditions

-20°C or -80°C if preferred

Shipping conditions

Ambient (domestic); Wet ice (international)

Product Specific Information

Reconstitute the lyophilized antibody with deionized water to the final concentration of 0.5 mg/ml.

GenScript THE™ His Tag Antibody [HRP], mAb, Mouse is HRP conjugated THE™ Anti-His Monoclonal Antibody (Mouse) (A00186) purified from mice ascites by protein A affinity column. This product is suitable for detecting the expression level of His fusion proteins or His by various immunoassays.

Target Information

The 6x His tag is a synthetic oligo peptide consisting of 6 consecutive histidine residues (HHHHHH). The His tag is commonly expressed as a tag at either N-or C-terminal regions of recombinant proteins to allow isolation or purification by immobilized metal affinity chromatography. Epitope tagging is a technique in which a known epitope is fused to a recombinant protein using genetic engineering. By choosing a particular epitope and recombinant protein combination, epitope tagging makes it possible to detect proteins for which no antibody is available. His epitope tagged proteins that contain a stretch of histidine residues at the carboxyl or amino terminus are used for purification of recombinant proteins by means of metal chelate chromatography due to metal binding properties of histidine clusters on His tagged proteins. For example, the affinity of the histidine-tag motif to Ni2+ by chelation is strong and selective enough to enable purification of the protein to homogeneity by affinity chromatography on a Ni2+-NTA adsorbent. His tag-specific antibodies are used to facilitate detection or coimmunopreciptation of tagged proteins.

⚠WARNING: This product can expose you to chemicals including mercury, which is known to the State of California to cause birth defects or other reproductive harm. For more information go to www.P65Warnings.ca.gov.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

Product References

ARTEMIS: A Novel Mass-Spec Platform for HLA-Restricted Self and Disease-Associated Peptide Discovery.

Frontiers in immunology

Finton KAK,Brusniak MY,Jones LA,Lin C,Fioré-Gartland AJ,Brock C,Gafken PR,Strong RK

Conventional immunoprecipitation/mass spectroscopy identification of HLA-restricted peptides remains the purview of specializing laboratories, due to the complexity of the methodology, and requires computational post-analysis to assign peptides to individual alleles when using pan-HLA antibodies. We have addressed these limitations with ARTEMIS: a simple, robust, and flexible platform for peptide discovery across ligandomes, optionally including specific proteins-of-interest, that combines novel

Tue Sep 28 00:00:00 UTC 2021

Conversion of the molecular chaperone Spy into a novel fusion tag to enhance recombinant protein expression.

Journal of biotechnology

Ruan A,Ren C,Quan S

The soluble expression of recombinant proteins in Escherichia coli is vital for protein applications in biotechnology and pharmaceuticals. However, the use of E. coli for efficient heterologous protein expression is hampered by several factors, such as poor expression and protein aggregation. Changing the culture or purification conditions may alleviate these issues, but methods based on gene fusion technology offer unique opportunities to improve the production and purification of soluble prote

Fri Jan 10 00:00:00 UTC 2020

SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2.

bioRxiv : the preprint server for biology

Clausen TM,Sandoval DR,Spliid CB,Pihl J,Painter CD,Thacker BE,Glass CA,Narayanan A,Majowicz SA,Zhang Y,Torres JL,Golden GJ,Porell R,Garretson AF,Laubach L,Feldman J,Yin X,Pu Y,Hauser B,Caradonna TM,Kellman BP,Martino C,Gordts PLSM,Leibel SL,Chanda SK,Schmidt AG,Godula K,Jose J,Corbett KD,Ward AB,Carlin AF,Esko JD

We show that SARS-CoV-2 spike protein interacts with cell surface heparan sulfate and angiotensin converting enzyme 2 (ACE2) through its Receptor Binding Domain. Docking studies suggest a putative heparin/heparan sulfate-binding site adjacent to the domain that binds to ACE2. In vitro, binding of ACE2 and heparin to spike protein ectodomains occurs independently and a ternary complex can be generated using heparin as a template. Contrary to studies with purified components, spike protein binding

Tue Jul 14 00:00:00 UTC 2020

Glycoprotein G (gG) production profile during infectious laryngotracheitis virus (ILTV) infection.

PloS one

Bendezu J,Morales Ruiz S,Montesinos R,Choque Guevara R,Rojas-Neyra A,Pauyac-Antezana K,Fernández-Díaz M

Glycoprotein G (gG) is a conserved protein, and it has been described as a chemokine-binding protein in most members of the alphaherpesviruses. In case of the infectious laryngotracheitis virus (ILTV), an alphaherpesvirus that infects chickens, this protein is a virulence factor that plays an immunomodulatory role in the chicken immune response. Nevertheless, the gG production profile during ILTV infection has not yet been studied. In this study, we developed monoclonal antibodies in order to de

Fri Feb 28 00:00:00 UTC 2020

Integrating SpyCatcher/SpyTag covalent fusion technology into phage display workflows for rapid antibody discovery.

Scientific reports

Fierle JK,Abram-Saliba J,Brioschi M,deTiani M,Coukos G,Dunn SM

An early bottleneck in the rapid isolation of new antibody fragment binders using in vitro library approaches is the inertia encountered in acquiring and preparing soluble antigen fragments. In this report we describe a simple yet powerful strategy that exploits the properties of the SpyCatcher/SpyTag (SpyC/SpyT) covalent interaction to improve substantially the speed and efficiency in obtaining functional antibody clones of interest. We demonstrate that SpyC has broad utility as a protein-fusio

Fri Sep 06 00:00:00 UTC 2019

Atomic insights into the genesis of cellular filaments by globular proteins.

Nature structural & molecular biology

McPartland L,Heller DM,Eisenberg DS,Hochschild A,Sawaya MR

Self-assembly of proteins into filaments, such as actin and tubulin filaments, underlies essential cellular processes in all three domains of life. The early emergence of filaments in evolutionary history suggests that filament genesis might be a robust process. Here we describe the fortuitous construction of GFP fusion proteins that self-assemble as fluorescent polar filaments in Escherichia coli. Filament formation is achieved by appending as few as 12 residues to GFP. Crystal structures revea

Wed Aug 01 00:00:00 UTC 2018

Structural and functional analysis of the GABARAP interaction motif (GIM).

EMBO reports

Rogov VV,Stolz A,Ravichandran AC,Rios-Szwed DO,Suzuki H,Kniss A,Löhr F,Wakatsuki S,Dötsch V,Dikic I,Dobson RC,McEwan DG

Through the canonical LC3 interaction motif (LIR) [W/F/Y]-X-X-[I/L/V] protein complexes are recruited to autophagosomes to perform their functions as either autophagy adaptors or receptors. How these adaptors/receptors selectively interact with either LC3 or GABARAP families remains unclear. Herein we determine the range of selectivity of 30 known core LIR motifs towards individual LC3s and GABARAPs. From these we define a ABARAP nteraction otif (GIM) sequence ([W/F]-[V/I]-X-V) that the adapt

Tue Aug 01 00:00:00 UTC 2017

Enhanced immunogenicity of HIV-1 envelope gp140 proteins fused to APRIL.

PloS one

Isik G,Sliepen K,van Montfort T,Sanders RW

Current HIV-1 vaccines based on the HIV-1 envelope glycoprotein spike (Env), the only relevant target for broadly neutralizing antibodies, are unable to induce protective immunity. Env immunogenicity can be enhanced by fusion to costimulatory molecules involved in B cell activation, such as APRIL and CD40L. Here, we found that Env-APRIL signaled through the two receptors, BCMA and TACI. In rabbits, Env-APRIL induced significantly higher antibody responses against Env compared to unconjugated Env

Mon Jun 22 00:00:00 UTC 2015

Bioinformatics

Protein Aliases: 6His tag; 6X His; His Tag; Histidine Tag

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