SSR1 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P43307 |
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Clone Names | 70319147 |
Gene ID | 6745 |
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Other Names | Translocon-associated protein subunit alpha, TRAP-alpha, Signal sequence receptor subunit alpha, SSR-alpha, SSR1, TRAPA |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP1444a was selected from the N-term region of human SSR1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | SSR1 |
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Synonyms | TRAPA |
Function | TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins. |
Cellular Location | Endoplasmic reticulum membrane; Single-pass type I membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum (ER) membrane receptor associated with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein encoded by this gene and a 22-kD glycoprotein. This gene generates several mRNA species as a result of complex alternative polyadenylation. This gene is unusual in that it utilizes arrays of polyA signal sequences that are exclusively non-canonical.
References
Hirama, T., et al., FEBS Lett. 455(3):223-227 (1999).Hartmann, E., et al., FEBS Lett. 349(3):324-326 (1994).
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