Recombinant Human SAHH Protein

Name: Recombinant Human SAHH Protein
Brand: Beta LifeScience
SKU: BLA-7995P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P23526
Synonym	Adenosylhomocysteinase AdoHcyase ahcY S adenosyl L homocysteine hydrolase S adenosylhomocysteine hydrolase S-adenosyl-L-homocysteine hydrolase SAHH SAHH_HUMAN
Description	Recombinant Human SAHH Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHHSSGLVPRGSHMSDKLPYKVADIGLAAWGRKALDIAENEMP GLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCN IFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDGPLNMILD DGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQ ALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCID IILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRL KNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYP VGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHY RY
Molecular Weight	50 kDa including tags
Purity	>95% purity as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycle.

Target Details

Target Function	Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Subcellular Location	Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Families	Adenosylhomocysteinase family
Database References	HGNC: 343 OMIM: 180960 KEGG: hsa:191 STRING: 9606.ENSP00000217426 UniGene: Hs.388004
Associated Diseases	Hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD)

Gene Functions References

Results uncover a H19/SAHH circuit involving gene-methylation alterations by carcinogen BaP. PMID: 29772428
We investigated previously assumed interaction with AHCY-like-1 protein (AHCYL1), a paralog of AHCY. Indeed, significant interaction between both proteins exists. Additionally, silencing AHCYL1 leads to moderate inhibition of nuclear export of endogenous AHCY. PMID: 28647132
We have validated the vectors and confirmed self-association of AHCY, AHCYL1, and galectin-3. In a high-throughput BiFC screen, we identified new AHCY interaction partners: galectin-3 and PUS7L. We also describe additional steps in protein interaction analysis, applied for AHCY-galectin-3 interaction PMID: 27455993
In order to enable the development of small molecule AHCY inhibitors as targeted cancer therapeutics we developed an assay based on a RapidFire high-throughput mass spectrometry detection system, which allows the direct measurement of AHCY enzymatic activity. PMID: 28533090
SAH hydrolase deficiency can remain asymptomatic in childhood, and the disorder can be associated with early onset hepatocellular carcinoma. PMID: 26527160
H19 knockdown activates SAHH, leading to increased DNMT3B-mediated methylation of an lncRNA-encoding gene Nctc1 within the Igf2-H19-Nctc1 locus. PMID: 26687445
S-adenosylhomocysteine hydrolase is regulated by lysine acetylation PMID: 25248746
SAHH can promote apoptosis, inhibit migration and adhesion of ESCC cells suggesting that it may be involved in carcinogenesis of the esophagus. PMID: 24430301
A fluorescence-based assay for the measurement of S-adenosylhomocysteine hydrolase activity in biological samples. PMID: 23079506
The simulations of ligand-induced transition revealed that the signal of intrasubunit closure dynamics is transmitted to form intersubunit contacts, which in turn invoke a precise alignment of active site. PMID: 22023331
Five active site residues (E156, N181, K186, D190, N191) of AdoHcy hydrolase have been individually mutated to alanine and each engineered enzyme characterized with respect to its redox partial reaction and elimination/addition partial reaction. PMID: 12069606
a discussion of its hydrolytic activity (review) PMID: 12369977
Maintenance of ionizable active-site residues in catalytically suitable protonation states in closed forms of placental AHCY may be assisted by a water chain, stabilized by Asp182, that can import and export protons from and to the environment. PMID: 12590576
AdoHcy is involved in adenosine-induced apoptosis by altering gene expression. PMID: 17097637
R38W and G123R amino-acid exchanges did not bring about major changes to the catalytic rates. However, circular dichroism analysis showed that both polymorphisms effect the thermal stability. PMID: 17164794
SAHH, which is diffuse in the cytoplasm of nonmotile Dictyostelium amoebae and human neutrophils, concentrates with F-actin in pseudopods at the front of motile, chemotaxing cells PMID: 17172447
In the case of Hs-SAHH, the slow-binding phase terminates in micromolar affinity, but over a period of hours, the dissociation rate constant decreases until the final equilibrium affinity is in the nanomolar range. PMID: 17447732
We found clinically relevant levels of Hcy (0-500 microM) induced elevation of SAH, declination of SAM and SAM/SAH ratio and reduced expression of SAHH and MBD2, but increased activity of DNMT3a and DNMT3b affecting DNA methylation PMID: 17688412
The mechanism of action of copper on this enzyme sugges a regulative role for copper on the intracellular activity. PMID: 17892301
consider changes in charge and the sterical incompatibility in mutant p.A89V protein as main reason for enzyme malfunction with AdoHcyase deficiency as consequence PMID: 18211827
SAHH from Homo sapiens (Hs-SAHH) and from the parasite Trypanosoma cruzi (Tc-SAHH) are very similar in structure and catalytic properties but differ in the kinetics and thermodynamics of association and dissociation of the cofactor NAD (+) PMID: 18393535
Streptococcal pyrogenic exotoxin B (SPE B) potentially causes immunosuppression by cleaving human S-adenosylhomocysteine hydrolase (AdoHcyase). PMID: 18522500
increased plasma concentration in patients with idiopathic thrombocytopenic purpura PMID: 18683034
SAHH mRNA was lost in 50% of tumor tissues from 206 patients with different kinds of tumors in comparison with normal tissue counterparts. Moreover, SAHH protein was also affected in some colon cancers PMID: 18713839
These data show that 2-5-fold enhanced AdoHcyase activity is well tolerated by the cell, while greatly enhanced AdoHcyase activity results in adenosine-induced apoptosis. PMID: 18769049
S-adenosylhomocysteine hydrolase PMID: 19619139

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.