GRP75/HSPA9B/Mortalin Recombinant Protein Antigen Summary
Description |
A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human HSPA9. Source: E. coli
Amino Acid Sequence: GIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGT Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)
This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions. |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein Antigen |
Gene |
HSPA9 |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- Antibody Competition 10 - 100 molar excess
|
Application Notes |
This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP1-89729. It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml. For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com |
Theoretical MW |
33 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at -20C. Avoid freeze-thaw cycles. |
Buffer |
PBS and 1M Urea, pH 7.4. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Alternate Names for GRP75/HSPA9B/Mortalin Recombinant Protein Antigen
Background
The HSP 70 family comprises four highly conserved proteins, HSP 70, HSC 70, GRP 75 and GRP 78, which serve a variety of roles. They act as molecular chaperones facilitating the assembly of multi-protein complexes, participate in the translocation of polypeptides across cell membranes and to the nucleus, and aid in the proper folding of nascent polypeptide chains. HSC 70, GRP 75 and GRP 78 are constitutively expressed in primate cells. HSP 70 expression is strongly induced in response to heat stress. HSP 70 and HSC 70, which are found in both the cytosol and nucleus of mammalian cells, play key roles in the cytosolic endoplasmic reticulum and mitochondrial import machinery. They are involved in chaperoning nascent polypeptide chains and in protecting cells against the accumulation of improperly folded proteins. GRP 75 and GRP 78 are unresponsive to heat stress and are induced by glucose deprivation. GRP 75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. GRP 78 is localized in the endoplasmic reticulum, where it receives imported secretory proteins and is involved in the folding and translocation of nascent peptide chains. Research indicates that members of the HSP 70 family may act as force-generating motors, relying on the hydrolysis of ATP for their activity.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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