Product Details

Full Product Name

Rabbit anti-Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SSB1 Polyclonal antibody

Uniprot No.

P11484

Target Names

SSB1

Alternative Names

SSB1 antibody; YG101 antibody; YDL229W antibody; Ribosome-associated molecular chaperone SSB1 antibody; EC 3.6.4.10 antibody; Cold-inducible protein YG101 antibody; Heat shock protein SSB1 antibody; Hsp70 chaperone Ssb antibody

Raised in

Rabbit

Species Reactivity

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Immunogen

Recombinant Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SSB1 protein

Immunogen Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Conjugate

Non-conjugated

Clonality

Polyclonal

Isotype

IgG

Purification Method

Antigen Affinity Purified

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4

Form

Liquid

Tested Applications

ELISA, WB (ensure identification of antigen)

Protocols

ELISA Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Value-added Deliverables

① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);

Quality Guarantee

① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;

Lead Time

Made-to-order (14-16 weeks)

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Target Background

Function

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.

Gene References into Functions

A positively charged region in the alpha-helical lid domain of SSB is identified. It is strictly required for ribosome binding. Crosslinking shows that Ssb binds close to the tunnel exit via contacts with both, ribosomal proteins and rRNA, and that specific contacts can be correlated with switching between the open (ATP-bound) and closed (ADP-bound) conformation. PMID: 27882919
Data show that the absence of either Ssb1/2 or Sch9 causes enhanced ribosome aggregation. PMID: 29038496
Study reveals molecular features of chaperone action during translation in eukaryotes by providing proteome-wide Ssb (two isoforms Ssb1 and Ssb2) interaction profiles with nascent chains at near-codon resolution. The Ssb interactome is broader than previously thought and includes nascent mitochondrial and endoplasmic reticulum- (ER) translocated proteins. PMID: 28708998
the ribosome-associated Hsp70 Ssb is redistributed away from Sup35 prion aggregates to the nascent chains, leading to an array of aggregation phenotypes that can mimic both overexpression and deletion of Ssb. PMID: 27828954
Study finds that SSB (i.e. closely related isoforms Ssb1 and Ssb2) binds to a subset of nascent polypeptides whose intrinsic properties and slow translation rates hinder efficient cotranslational folding. PMID: 23332755
The ribosome-bound chaperone system consisting of the ribosome-associated complex (RAC) and the Hsp70 homologs SSB1 and SSB2 are required to stabilize translationally repressed ribosome-polylysine protein complexes. PMID: 23007158
Results suggest that RAC and Ssb1/2p are crucial in maintaining translational fidelity beyond their postulated role as chaperones for nascent polypeptides. PMID: 15456889
ssb and zuo1 have a role in cation influx in Saccharomyces cerevisiae membranes PMID: 15643063
A plausible role of the Ssb1 chaperone is to stabilize genetic networks, thus making them more tolerant to malfunctioning of their constituents. PMID: 16849597
Zuo1 and Ssz1 together with the Hsp70 homolog Ssb1/2 form a functional triad involved in translation and early polypeptide folding processes. PMID: 17901048

Hide All

Subcellular Location

Cytoplasm.

Protein Families

Heat shock protein 70 family, Ssb-type Hsp70 subfamily

Database Links

KEGG: sce:YDL229W

STRING: 4932.YDL229W

Message

Product >> Product Name：
Product >> Code：
Name： *
Email： *
Company/Organization：
Phone：
Since emails may get flagged by spam filters occasionally, we recommend leaving your phone number as a precaution. Your information is safe with us.
Question/Comment： *
Your Region： *
I'd like to receive email newsletters from Cusabio

Yes

No
How do you know CUSABIO?

Email

Distributor

Search engine

Advertisement

Others
CAPTCHA verification：

Code	CSB-PA320875XA01SVG
Size	Enquire
Have Questions?	Leave a Message or Start an on-line Chat

SSB1 Antibody

Product Details

Related Products

Customer Reviews and Q&A

Target Background