Name: glnE Antibody
Brand: CUSABIO
SKU: CSB-PA330033XA01ENV

Product Details

Full Product Name

Rabbit anti-Escherichia coli (strain K12) glnE Polyclonal antibody

Uniprot No.

P30870

Target Names

glnE

Alternative Names

glnE antibody; b3053 antibody; JW3025Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme antibody; ATP:glutamine synthetase adenylyltransferase antibody; ATase) [Includes: Glutamine synthetase adenylyl-L-tyrosine phosphorylase antibody; EC 2.7.7.89 antibody; Adenylyl removase antibody; AR antibody; AT-N antibody; AT-N440 antibody; P-I); Glutamine synthetase adenylyl transferase antibody; EC 2.7.7.42 antibody; Adenylyl transferase antibody; AT antibody; AT-C)] antibody

Raised in

Rabbit

Species Reactivity

Escherichia coli (strain K12)

Immunogen

A synthesized peptide derived from Escherichia coli (strain K12) glnE protein

Immunogen Species

Escherichia coli (strain K12)

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, Dot blot (guaranteed specific to the immunizing peptide)

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. 100ug * KLH-conjugated peptide paired with 100ug * BSA-conjugated peptide (positive control);
②. 1ml*pre-immune serum (used as negative control) for free;
③. Rabbit polyclonal antibodies purified by Antigen Affinity;

Quality Guarantee

1. CUSABIO guarantees the antibody purity > 95% confirmed by SDS-PAGE.
2. CUSABIO guarantees the antibody titer > 1: 64,000 confirmed by ELISA.
3. CUSABIO guarantees to offer Peptide-specific Dot blot.
4. CUSABIO guarantees 100% risk-free: No qualified antibody, no charge.

Lead Time

Made-to-order (14-16 weeks)

Usage

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

Target Background

Function

Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.

Gene References into Functions

the adenylyl-removing (AR) activity of bifunctional GS adenylyltransferase/adenylyl-removing enzyme (ATase) is required to counterbalance its AT activity during steady-state growth under both nitrogen-excess and nitrogen-limiting conditions PMID: 20887734
The structures of the adenylyl transferase and adenylyl removase domains overlap with an rmsd of 2.4 A when the superhelical R domain is omitted. PMID: 20026075
Subtle alterations in the environment of glutamine synthetase side chain residue Tyr-397 are sufficient to induce changes previously thought to require adenylylation. PMID: 15996098
X-ray crystallographic analysis of the C-terminal domain of adenylyltransferase (ATase) from Escherichia coli PMID: 16511122
N-terminal NT domain contains adenylyl-removing active site, & C-terminal NT domain has adenylyltransferase active site; enzyme has glutamine binding site, & glutamine increases affinity for PII; it contains multiple sites for binding of PII & PII-UMP PMID: 17355124
adenylyltransferase (AT) reaction is activated by glutamine and by the unmodified form of the PII signal transduction protein and is inhibited by the uridylylated form of PII, PII-UMP. PMID: 17355125
A panel of mAbs to adenylyltransferase was used to demonstrate that the cellular nitrogen status indicators, PII and PII-UMP, probably bind in the central regulatory domain to stimulate the adenylylation and deadenylylation reactions, respectively. PMID: 17488285

Hide All

Protein Families

GlnE family

Database Links

KEGG: ecj:JW3025

STRING: 316385.ECDH10B_3228

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glnE Antibody

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