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1000 results found for “hepatitis d”
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Name :
DHH (C23II) His HumanDescription:
Desert HedgeHog (C23II) Human Recombinant, His Tag
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
Product # :
CYT-763Price :
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Description
DHH (C23II) His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (23-198) and having a molecular mass of 22.4kDa.DHH (C23II) His is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHH (C23II) His solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development. -
Synonyms
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMIIGPGR GPVGRRRYAR KQLVPLLYKQ FVPGVPERTL GASGPAEGRV ARGSERFRDL VPNYNPDIIF KDEENSGADR LMTERCKERV NALAIAVMNM WPGVRLRVTE GWDEDGHHAQ DSLHYEGRAL DITTSDRDRN KYGLLARLAV EAGFDWVYYE SRNHVHVSVK ADNSLAVRAG G
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DLL4 HumanDescription:
Delta-Like 4 Human Recombinant
Delta-like protein 4, Drosophila Delta homolog 4, Delta4, delta like canonical Notch ligand 4, AOS6, hdelta2.
Product # :
PRO-2660Price :
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Description
DLL4 Human Recombinant produced in HEK293 is a single glycosylated polypeptide chain containing 504 amino acids (27-529 a.a) and having a molecular mass of 55.1kDa. DLL4 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293.
Formulation
DLL4 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Delta-Like4 or DLL4 is implicated in the Notch signaling transduction as Notch ligand. DLL4 down regulates endothelial cell proliferation, migration and angiogenic sprouting. DLL4 is crucial for retinal progenitor proliferation &furthermore required for suppressing rod fates in late retinal progenitors & for proper generation of other retinal cell types. Also, at some stages in the spinal cord neurogenesis, DLL4 inhibits V2a interneuron fate.
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Synonyms
Delta-like protein 4, Drosophila Delta homolog 4, Delta4, delta like canonical Notch ligand 4, AOS6, hdelta2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
SGVFQLQLQE FINERGVLAS GRPCEPGCRT FFRVCLKHFQ AVVSPGPCTF GTVSTPVLGT NSFAVRDDSS GGGRNPLQLP FNFTWPGTFS LIIEAWHAPG DDLRPEALPP DALISKIAIQ GSLAVGQNWL LDEQTSTLTR LRYSYRVICS DNYYGDNCSR LCKKRNDHFG HYVCQPDGNL SCLPGWTGEY CQQPICLSGC HEQNGYCSKP AECLCRPGWQ GRLCNECIPH NGCRHGTCST PWQCTCDEGW GGLFCDQDLN YCTHHSPCKN GATCSNSGQR SYTCTCRPGY TGVDCELELS ECDSNPCRNG GSCKDQEDGY HCLCPPGYYG LHCEHSTLSC ADSPCFNGGS CRERNQGANY ACECPPNFTG SNCEKKVDRC TSNPCANGGQ CLNRGPSRMC RCRPGFTGTY CELHVSDCAR NPCAHGGTCH DLENGLMCTC PAGFSGRRCE VRTSIDACAS SPCFNRATCY TDLSTDTFVC NCPYGFVGSR CEFPVGLPHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DBNDD1 HumanDescription:
Dysbindin (Dystrobrevin Binding Protein 1) Domain Containing 1 Human Recombinant
Dysbindin domain-containing protein 1, DBNDD1.
Product # :
PRO-1162Price :
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Description
DBNDD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-158 a.a) and having a molecular mass of 19.6kDa (Molecular weight on SDS-PAGE will appear higher).DBNDD1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DBNDD1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Dysbindin domain-containing protein 1 (DBNDD1) is a member of the dysbindin family.
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Synonyms
Dysbindin domain-containing protein 1, DBNDD1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEPPEG AGTGEIVKEA EVPQAALGVP AQGTGDNGHT PVEEEVGGIP VPAPGLLQVT ERRQPLSSVS SLEVHFDLLD LTELTDMSDQ ELAEVFADSD DENLNTESPA GLHPLPRAGY LRSPSWTRTR AEQSHEKQPL GDPERQATVL DTFLTVERPQ ED.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SDHAF2 HumanDescription:
Succinate Dehydrogenase Complex Assembly Factor 2 Human Recombinant
Succinate dehydrogenase assembly factor 2 mitochondrial, SDH assembly factor 2, Succinate dehydrogenase subunit 5, mitochondrial, hSDH5, SDHAF2, C11orf79, PGL2, SDH5.
Product # :
PRO-593Price :
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Shipped with Ice Packs
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Description
SDHAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (30-166 a.a) and having a molecular mass of 19kDa.SDHAF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDHAF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Succinate Dehydrogenase Complex Assembly Factor 2 (SDHAF2) is a mitochondrial protein required for the flavination of a succinate dehydrogenase complex subunit essential for activity of the complex. DHAF2 is necessary for insertion of FAD cofactor into SDHA, the catalytic subunit of succinate dehydrogenase (SDH). SDH is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDHAF2 gene defects are the cause of hereditary paragangliomas type 2 (PGL2), otherwise known as familial non-chromaffin paragangliomas type 2.
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Synonyms
Succinate dehydrogenase assembly factor 2 mitochondrial, SDH assembly factor 2, Succinate dehydrogenase subunit 5, mitochondrial, hSDH5, SDHAF2, C11orf79, PGL2, SDH5.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSFRRFYR GDSPTDSQKD MIEIPLPPWQ ERTDESIETK RARLLYESRK RGMLENCILL SLFAKEHLQH MTEKQLNLYD RLINEPSNDW DIYYWATEAK PAPEIFENEV MALLRDFAKN KNKEQRLRAP DLEYLFEKPR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DTYMK HumanDescription:
Deoxythymidylate Kinase Human Recombinant
Deoxythymidylate Kinase (Thymidylate Kinase), DTMP Kinase, CDC8, TMPK, TYMK, Thymidylate (DTMP) Kinase, EC 2.7.4.9, PP3731, Thymidylate kinase.
Product # :
PKA-005Price :
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Description
DTYMK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212 a.a) and having a molecular mass of 26kDa. DTYMK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
DTYMK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thymidylate kinase (DTYMK) is involved in pyrimidine metabolism. Specifically, DTYMK catalyzes the ATP-dependent conversion of dTMP (deoxythymidine monophosphate) to dTDP (deoxythymidine diphosphate), which then acts as one of the 4 nucleotides in DNA. Through its role in the catalytic creation of dTDP, DTYMK has an imperative role in the pathway of DNA synthesis and is assumed to be involved in cell cycle progression and cell growth.
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Synonyms
Deoxythymidylate Kinase (Thymidylate Kinase), DTMP Kinase, CDC8, TMPK, TYMK, Thymidylate (DTMP) Kinase, EC 2.7.4.9, PP3731, Thymidylate kinase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA SKSIEAVHED IRVLSEDAIR TATEKPLGEL WK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IDO1 HumanDescription:
Indoleamine 2,3-Dioxygenase 1 Human Recombinant
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
Product # :
ENZ-807Price :
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Shipped with Ice Packs
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Description
IDO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403a.a) and having a molecular mass of 47.7kDa. IDO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDO1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.
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Synonyms
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAHAMEN SWTISKEYHI DEEVGFALPN PQENLPDFYN DWMFIAKHLP DLIESGQLRE RVEKLNMLSI DHLTDHKSQR LARLVLGCIT MAYVWGKGHG DVRKVLPRNI AVPYCQLSKK LELPPILVYA DCVLANWKKK DPNKPLTYEN MDVLFSFRDG DCSKGFFLVS LLVEIAAASA IKVIPTVFKA MQMQERDTLL KALLEIASCL EKALQVFHQI HDHVNPKAFF SVLRIYLSGW KGNPQLSDGL VYEGFWEDPK EFAGGSAGQS SVFQCFDVLL GIQQTAGGGH AAQFLQDMRR YMPPAHRNFL CSLESNPSVR EFVLSKGDAG LREAYDACVK ALVSLRSYHL QIVTKYILIP ASQQPKENKT SEDPSKLEAK GTGGTDLMNF LKTVRSTTEK SLLKEG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OLA1 HumanDescription:
Obg-Like ATPase 1 Human Recombinant
Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.
Product # :
ENZ-637Price :
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Shipped with Ice Packs
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Description
OLA1 Human Recombinant produced in E. coli is a single polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 47.3kDa.OLA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OLA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.
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Synonyms
Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPPKKG GDGIKPPPII GRFGTSLKIG IVGLPNVGKS TFFNVLTNSQ ASAENFPFCT IDPNESRVPV PDERFDFLCQ YHKPASKIPA FLNVVDIAGL VKGAHNGQGL GNAFLSHISA CDGIFHLTRA FEDDDITHVE GSVDPIRDIE IIHEELQLKD EEMIGPIIDK LEKVAVRGGD KKLKPEYDIM CKVKSWVIDQ KKPVRFYHDW NDKEIEVLNK HLFLTSKPMV YLVNLSEKDY IRKKNKWLIK IKEWVDKYDP GALVIPFSGA LELKLQELSA EERQKYLEAN MTQSALPKII KAGFAALQLE YFFTAGPDEV RAWTIRKGTK APQAAGKIHT DFEKGFIMAE VMKYEDFKEE GSENAVKAAG KYRQQGRNYI VEDGDIIFFK FNTPQQPKKK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PDPN HumanDescription:
Podoplanin Human Recombinant
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
Product # :
PRO-626Price :
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Shipped with Ice Packs
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Description
PDPN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (99-207 a.a) and having a molecular mass of 13.4kDa. PDPN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl pH7.5 & 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors. -
Synonyms
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASTGQPEDD TETTGLEGGV AMPGAEDDVV TPGTSEDRYK SGLTTLVATS VNSVTGIRIE DLPTSESTVH AQEQSPSATA SNVATSHSTE KVDGDTQTTV EKDGLSTVTL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TrxR YeastDescription:
Thioredoxin Reductase (NADPH) Yeast Recombinant
Thioredoxin Reductase (NADPH), NTR, TrxR.
Product # :
ENZ-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of protein contains 20mM phosphate buffer pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 5.8 IU/mg.
Citations
More Info
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Introduction
Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.
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Synonyms
Thioredoxin Reductase (NADPH), NTR, TrxR.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.
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Unit Definition
One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2E3 HumanDescription:
Ubiquitin Conjugating Enzyme E2E3 Human Recombinant
UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.
Product # :
ENZ-906Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UBE2E3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-207 a.a) and having a molecular mass of 25.3kDa.UBE2E3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2E3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
UBE2E3 or Ubiquitin-conjugating enzyme E2 E3 is part of the E2 ubiquitinconjugating enzyme family. UBE2E3 is needed for the destruction of mitotic cyclins and for cell cycle progression. The ubiquitination process covalently attaches to a short protein of 76 amino acids called ubiquitin, to a lysine residue on the target protein. When a protein has been tagged with one ubiquitin molecule, other rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein which grants passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.
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Synonyms
UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSDRQR SDDESPSTSS GSSDADQRDP AAPEPEEQEE RKPSATQQKK NTKLSSKTTA KLSTSAKRIQ KELAEITLDP PPNCSAGPKG DNIYEWRSTI LGPPGSVYEG GVFFLDITFS SDYPFKPPKV TFRTRIYHCN INSQGVICLD ILKDNWSPAL TISKVLLSIC SLLTDCNPAD PLVGSIATQY LTNRAEHDRI ARQWTKRYAT.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HK2 AntibodyDescription:
Hexokinase-2, Mouse Anti Human
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
Product # :
ANT-378Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
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Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.
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Synonyms
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
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Immunogen
Anti-human Hexokinase-2 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Hexokinase-2 amino acids 1-917 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P1A7AT.
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Applications
Hexokinase-2 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 3,000. Recommended starting dilution is 1:2,000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
Hexokinase-2 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
N6AMT1 HumanDescription:
N-6 Adenine-Specific DNA Methyltransferase 1 Human Recombinant
N-6 Adenine-Specific DNA Methyltransferase 1 (Putative), N(6)-Adenine-Specific DNA Methyltransferase 1, HemK Methyltransferase Family Member 2, M.HsaHemK2P, C21orf127, HEMK2, Chromosome 21 Open Reading Frame 127, N6-DNA-Methyltransferase, EC 2.1.1.- , PRED28, N6AMT, MTQ2, HemK methyltransferase family member 2.
Product # :
ENZ-834Price :
Quantity :
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Description
N6AMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 25.3kDa. N6AMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
N6AMT1 protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
N-6 Adenine-Specific DNA Methyltransferase 1, also known as N6AMT1 is part of the methyltransferase family. N6AMT1 is implicated in the methylation of release factor I during translation termination. In addition, N6AMT1 is involved in converting the arsenic metabolite monomethylarsonous acid to the less toxic dimethylarsonic acid.
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Synonyms
N-6 Adenine-Specific DNA Methyltransferase 1 (Putative), N(6)-Adenine-Specific DNA Methyltransferase 1, HemK Methyltransferase Family Member 2, M.HsaHemK2P, C21orf127, HEMK2, Chromosome 21 Open Reading Frame 127, N6-DNA-Methyltransferase, EC 2.1.1.- , PRED28, N6AMT, MTQ2, HemK methyltransferase family member 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAGENFA TPFHGHVGRG AFSDVYEPAE DTFLLLNALE AAAAELAGVE ICLEVGSGSG VVSAFLASMI GPQALYMCTD INPEAAACTL ETARCNKVHI QPVITDLVKG LLPRLTEKVD LLVFNPPYVV TPPQEVGSHG IEAAWAGGRN GREVMDRFFP LVPDLLSPRG LFYLVTIKEN NPEEILKIMK TKGLQGTTAL SRQAGQETLS VLKFTKS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TDP1 Human, Sf9Description:
Tyrosyl-DNA Phosphodiesterase 1 Human Recombinant, Sf9
Tyrosyl-DNA phosphodiesterase 1, Tyr-DNA phosphodiesterase 1, TDP1, FLJ11090, MGC104252.
Product # :
ENZ-1038Price :
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Description
TDP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 617 amino acids (1-608) and having a molecular mass of 69.5kDa. TDP1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TDP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TDP1 belongs to the phospholipase D family and contains two PLD phosphodiesterase domains. TDP1 is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 may also remove glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks. Mutations in the TDP1 gene are linked to the disease spinocerebellar ataxia with axonal neuropathy (SCAN1).
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Synonyms
Tyrosyl-DNA phosphodiesterase 1, Tyr-DNA phosphodiesterase 1, TDP1, FLJ11090, MGC104252.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPMSQEGDY GRWTISSSDE SEEEKPKPDK PSTSSLLCAR QGAANEPRYT CSEAQKAAHK RKISPVKFSN TDSVLPPKRQ KSGSQEDLGW CLSSSDDELQ PEMPQKQAEK VVIKKEKDIS APNDGTAQRT ENHGAPACHR LKEEEDEYET SGEGQDIWDM LDKGNPFQFY LTRVSGVKPK YNSGALHIKD ILSPLFGTLV SSAQFNYCFD VDWLVKQYPP EFRKKPILLV HGDKREAKAH LHAQAKPYEN ISLCQAKLDI AFGTHHTKMM LLLYEEGLRV VIHTSNLIHA DWHQKTQGIW LSPLYPRIAD GTHKSGESPT HFKADLISYL MAYNAPSLKE WIDVIHKHDL SETNVYLIGS TPGRFQGSQK DNWGHFRLKK LLKDHASSMP NAESWPVVGQ FSSVGSLGAD ESKWLCSEFK ESMLTLGKES KTPGKSSVPL YLIYPSVENV RTSLEGYPAG GSLPYSIQTA EKQNWLHSYF HKWSAETSGR SNAMPHIKTY MRPSPDFSKI AWFLVTSANL SKAAWGALEK NGTQLMIRSY ELGVLFLPSA FGLDSFKVKQ KFFAGSQEPM ATFPVPYDLP PELYGSKDRP WIWNIPYVKA PDTHGNMWVP SHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
POR Human, ActiveDescription:
P450 Oxidoreductase Human Recombinant, Active
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
Product # :
ENZ-1176Price :
Quantity :
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Description
POR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 686 amino acids (1-680a.a.) and having a molecular mass of 77.9kDa. POR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 4,000 pmol/min/mg. Defined by the amount of enzyme that reduction of 1 pmole cytochrome-C by NADPH/min. at pH-8 25C.
Citations
More Info
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Introduction
P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.
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Synonyms
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MINMGDSHVD TSSTVSEAVA EEVSLFSMTD MILFSLIVGL LTYWFLFRKK KEEVPEFTKI QTLTSSVRES SFVEKMKKTG RNIIVFYGSQ TGTAEEFANR LSKDAHRYGM RGMSADPEEY DLADLSSLPE IDNALVVFCM ATYGEGDPTD NAQDFYDWLQ ETDVDLSGVK FAVFGLGNKT YEHFNAMGKY VDKRLEQLGA QRIFELGLGD DDGNLEEDFI TWREQFWLAV CEHFGVEATG EESSIRQYEL VVHTDIDAAK VYMGEMGRLK SYENQKPPFD AKNPFLAAVT TNRKLNQGTE RHLMHLELDI SDSKIRYESG DHVAVYPAND SALVNQLGKI LGADLDVVMS LNNLDEESNK KHPFPCPTSY RTALTYYLDI TNPPRTNVLY ELAQYASEPS EQELLRKMAS SSGEGKELYL SWVVEARRHI LAILQDCPSL RPPIDHLCEL LPRLQARYYS IASSSKVHPN SVHICAVVVE YETKAGRINK GVATNWLRAK EPVGENGGRA LVPMFVRKSQ FRLPFKATTP VIMVGPGTGV APFIGFIQER AWLRQQGKEV GETLLYYGCR RSDEDYLYRE ELAQFHRDGA LTQLNVAFSR EQSHKVYVQH LLKQDREHLW KLIEGGAHIY VCGDARNMAR DVQNTFYDIV AELGAMEHAQ AVDYIKKLMT KGRYSLDVWS HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IDE Human, ActiveDescription:
Insulin-Degrading Enzyme Human Recombinant
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
Product # :
ENZ-1192Price :
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Shipped with Ice Packs
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Description
IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa. IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDE solution (0.5mg/ml) contains 10% Glycerol, 100mM NaCl, 0.05% Brij35 and 20mM Tris-HCl buffer (pH 7.5).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is greater than 3,000 pmol/min/ug in which 1 unit will convert 1.0 pmole of Mca-RPPGFSAFK(Dnp)-OH to MCA-Pro-Leu-OH per minute at pH 7.5 at 25°C.
Citations
More Info
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Synonyms
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
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Physical Appearance
Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLISDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTAMSKLWF KQDDKFFLPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS
QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQGLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKLHH HHHH. -
Background
Insulin-degrading enzyme (IDE) is a crucial protease that plays a significant role in maintaining glucose homeostasis by degrading insulin and other bioactive peptides. Dysregulation of IDE has been implicated in various metabolic disorders, particularly type 2 diabetes mellitus. IDE is also associated with the clearance of amyloid-beta peptides in the brain, making it relevant to Alzheimer's disease pathology. Studying the recombinant form of IDE is fundamental to understanding its functional mechanisms and exploring potential avenues for therapeutic interventions.
The primary goal of this research is to express and purify recombinant IDE using diverse expression systems. Recombinant DNA techniques will be employed to construct expression vectors containing the IDE gene, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant IDE will be purified using affinity chromatography or other appropriate methods, facilitating subsequent biochemical and biophysical characterization.
The second objective is to investigate the substrate specificity and catalytic activity of the purified IDE. In vitro enzymatic assays will be conducted to analyse the ability of the recombinant IDE to degrade insulin and other potential substrates. The effects of various factors, such as pH, temperature, and potential modulators, on IDE activity will be evaluated. Additionally, the interactions between IDE and its substrates will be explored using binding assays.
The third objective is to elucidate the three-dimensional structure of the IDE recombinant using techniques like X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Structural insights into the active site and binding pockets of IDE will provide valuable information for understanding its substrate recognition and catalytic mechanisms. This knowledge could be instrumental in designing targeted therapeutic compounds.
By characterizing the IDE recombinant, this research aims to contribute to our understanding of its role in insulin metabolism, glucose regulation, and potential therapeutic applications. The findings from this study may have implications for the development of novel treatments for diabetes and other related disorders.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GPT2 Human, ActiveDescription:
Glutamic-Pyruvate Transaminase 2 Human Recombinant, Active
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
Product # :
ENZ-995Price :
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Shipped with Ice Packs
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Description
GPT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 546 amino acids (1-523) and having a molecular mass of 60.3 kDa. GPT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH7.5), 30% glycerol, 2mM DTT, 0.2M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.Citations
More Info
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Introduction
Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.
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Synonyms
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMQRAAAL VRRGCGPRTP SSWGRSQSSA AAEASAVLKV RPERSRRERI LTLESMNPQV KAVEYAVRGP IVLKAGEIEL ELQRGIKKPF TEVIRANIGD AQAMGQQPIT FLRQVMALCT YPNLLDSPSF PEDAKKRARR ILQACGGNSL GSYSASQGVN CIREDVAAYI TRRDGGVPAD PDNIYLTTGA SDGISTILKI LVSGGGKSRT GVMIPIPQYP LYSAVISELD AIQVNYYLDE ENCWALNVNE LRRAVQEAKD HCDPKVLCII NPGNPTGQVQ SRKCIEDVIH FAWEEKLFLL ADEVYQDNVY SPDCRFHSFK KVLYEMGPEY SSNVELASFH STSKGYMGEC GYRGGYMEVI NLHPEIKGQL VKLLSVRLCP PVSGQAAMDI VVNPPVAGEE SFEQFSREKE SVLGNLAKKA KLTEDLFNQV PGIHCNPLQG AMYAFPRIFI PAKAVEAAQA HQMAPDMFYC MKLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPVEKLKTV LQKVKDFHIN FLEKYA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TH MouseDescription:
Tyrosine Hydroxylase Mouse Recombinant
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.
Product # :
ENZ-988Price :
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Description
TH Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) and having a molecular mass of 57.0kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TH protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.
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Synonyms
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPMPTPSAS SPQPKGFRRA VSEQDTKQAE AVTSPRFIGR RQSLIEDARK EREAAAAAAA AAVASAEPGN PLEAVVFEER DGNAVLNLLF SLRGTKPSSL SRALKVFETF EAKIHHLETR PAQRPLAGSP HLEYFVRFEV PSGDLAALLS SVRRVSDDVR SAREDKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG EPIPHVEYTK EEIATWKEVY ATLKGLYATH ACREHLEAFQ LLERYCGYRE DSIPQLEDVS HFLKERTGFQ LRPVAGLLSA RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ FSQDIGLASL GASDEEIEKL STVYWFTVEF GLCKQNGELK AYGAGLLSSY GELLHSLSEE PEVRAFDPDT AAVQPYQDQT YQPVYFVSES FSDAKDKLRN YASRIQRPFS VKFDPYTLAI DVLDSPHTIR RSLEGVQDEL HTLTQALSAI SHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ASGR2 HumanDescription:
Asialoglycoprotein Receptor 2 Human Recombinant
Asialoglycoprotein receptor 2, ASGP-R 2, ASGPR 2, C-type lectin domain family 4 member H2, Hepatic lectin H2, HL-2, ASGR2, CLEC4H2, HBXBP.
Product # :
PRO-1261Price :
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Description
ASGR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (80-311 a.a) and having a molecular mass of 28.9kDa.ASGR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ASGR2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Asialoglycoprotein Receptor 2 (ASGR2) is a hetero-oligomeric protein comprised of major and minor subunits, encoded by different genes. ASGR2 is a subunit of the asialoglycoprotein receptor; it is the less abundant minor subunit. The ASGR2 receptor is a transmembrane protein, which has a crucial role in serum glycoprotein homeostasis by mediating the endocytosis and lysosomal degradation of glycoproteins with exposed terminal galactose or N-acetylgalactosamine residues.
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Synonyms
Asialoglycoprotein receptor 2, ASGP-R 2, ASGPR 2, C-type lectin domain family 4 member H2, Hepatic lectin H2, HL-2, ASGR2, CLEC4H2, HBXBP.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQSEGHRG AQLQAELRSL KEAFSNFSSS TLTEVQAIST HGGSVGDKIT SLGAKLEKQQ QDLKADHDAL LFHLKHFPVD LRFVACQMEL LHSNGSQRTC CPVNWVEHQG SCYWFSHSGK AWAEAEKYCQ LENAHLVVIN SWEEQKFIVQ HTNPFNTWIG LTDSDGSWKW VDGTDYRHNY KNWAVTQPDN WHGHELGGSE DCVEVQPDGR WNDDFCLQVY RWVCEKRRNA TGEVA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Hepsin HumanDescription:
Hepsin Human Recombinant
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
Product # :
PRO-2846Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Hepsin Human Recombinant produced in Cho cells is a covalently-linked heterodimer having a total molecular mass of 43.0kDa. Hepsin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
The Hepsin protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity is >20,000 pmol/min/μg and was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC).Citations
More Info
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Synonyms
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hepsin Active although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hepsin Active should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles. -
Solubility
It is recommended to reconstitute the lyophilized Hepsin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR.
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H.
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Background
Hepsin is a type II transmembrane serine protease expressed primarily on epithelial cells, it takes part in extracellular proteolysis by activating precursor proteins such as pro-HGF and contributes to tissue remodeling, cell signaling, and normal epithelial function. Recombinant Hepsin is used to study prostate cancer, extracellular matrix remodelling, protease signalling pathways, tumor invasion, metastasis, HGF/MET signaling, and for screening inhibitors that target serine proteases
What is the molecular weight / Mw of Hepsin Protein?
Hepsin Protein has a total Mw of 43kDa.
What is the source or expression system of Hepsin Protein?
CHO Cells
What is the Purity of Hepsin Protein?
Hepsin Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Hepsin Protein?
The enzymatic activity was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC). The specific activity is >20,000 pmol/min/μg.
What is the amino acid sequence of Hepsin Protein?
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H
What applications can Hepsin Protein be used in?
Hepsin Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for Hepsin Protein?
The endotoxin level is minimal, Hepsin Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ENO2 Human, HisDescription:
Enolase-2 Human Recombinant, His Tag
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Product # :
ENZ-298Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Neuron Specific Enolase Human Recombinant is expressed in E. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag.The NSE is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Enolase 2 is supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.Citations
More Info
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Introduction
NSE is the ?? isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival.
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Synonyms
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL13 Human, HisDescription:
Interleukin-13 Human Recombinant, His Tag
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
Product # :
CYT-489Price :
Quantity :
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Shipped with Ice Packs
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Description
Interleukin-13 His Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (21-132) having a molecular weight of 12.84kDa with a 4kDa amino-terminal hexahistidine tag (total weight of 16.84kDa). The IL-13 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin -13 His-Tag protein is supplied in 25mM Na-Acetate (pH 4.8) and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Interleukin-13 is a pleiotropic regulatory cytokine, which shares many of the properties of Interleukin-4. IL-13 is produced primarily by activated T lymphocytes and acts via specific cell surface receptor complexes. Its biological activities include the stimulation of B-cell proliferation and differentiation and the regulation of inflammatory and immune responses.
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Synonyms
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein has a total Mw of 12.8kDa.
What is the source or expression system of IL13 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL13 HUMAN, HIS Protein?
The biological functionality of IL13 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of IL13 HUMAN, HIS Protein?
IL13 HUMAN, HIS Protein is composed from 112 amino acids.
What applications can IL13 HUMAN, HIS Protein be used in?
IL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL13 HUMAN, HIS Protein?
The endotoxin level is minimal, IL13 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL13 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL13 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GAPDH Human, ActiveDescription:
Glyceraldehyde-3-Phosphate Dehydrogenase Human Recombinant, Active
G3PD, GAPD, MGC88685, GAPDH, Glyceraldehyde-3-Phosphate Dehydrogenase.
Product # :
ENZ-985Price :
Quantity :
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Description
GAPDH Human Recombinant produced in E. coli is a single polypeptide chain containing 335 amino acids (1-335) and having a molecular mass of 36kDa. The GAPDH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GAPDH protein (1 mg/ml) contains 20mM Tris-HCl buffer pH-8, 1mM EDTA, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 50 units/mg, and is defined as the amount of enzyme that convert 1.0 umole of glyceraldehyde-3-phosphate to 1,3-Bisphosphoglycerate per minute at pH 8.5 at 37C.
Citations
More Info
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Introduction
GAPDH is a catalytic enzyme normally known to play a role in glycolysis. GAPDH exists as a tetramer composed of 36-kDa subunits and has a range of intracellular functions. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, GAPDH has function in intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. GAPDH catalyzes a vital energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains.
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Synonyms
G3PD, GAPD, MGC88685, GAPDH, Glyceraldehyde-3-Phosphate Dehydrogenase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD STHGKFHGTV KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG VFTTMEKAGA HLQGGAKRVI ISAPSADAPM FVMGVNHEKY DNSLKIISNA SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA ITATQKTVDG PSGKLWRDGR GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV SVVDLTCRLE KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NDUFAF2 HumanDescription:
NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 2 Human Recombinant
Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.
Product # :
ENZ-150Price :
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Description
NDUFAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a.) and having a molecular mass of 22kDa.NDUFAF2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NDUFAF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Mimitin (NDUFAF2) is a member of the complex I NDUFA12 subunit family.NADH dehydrogenase is an enzyme located in the inner mitochondrial membrane, which catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NDUFAF2 is the "entry enzyme" of oxidative phosphorylation in the mitochondria. Mimitin protein functions as a molecular chaperone for mitochondrial complex I assembly.
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Synonyms
Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGWSQDLFRA LWRSLSREVK EHVGTDQFGN KYYYIPQYKN WRGQTIREKR IVEAANKKEV DYEAGDIPTE WEAWIRRTRK TPPTMEEILK NEKHREEIKI KSQDFYEKEK LLSKETSEEL LPPPVQTQIK GHASAPYFGK EEPSVAPSST GKTFQPGSWM PRDGKSHNQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CD300A HumanDescription:
CD300A Human Recombinant
CD300a Molecule, CD300a Antigen, IRp60, CD300 Antigen-Like Family Member A, NK Inhibitory Receptor, Immunoglobulin Superfamily Member 12, CMRF35-Like Molecule 8, CMRF35-H, Inhibitory Receptor Protein 60, CMRF-35-H9, CMRF-35H, CLM-8, IRC1, IRC2, CMRF35H Leukocyte Immunoglobulin-Like Receptor, Leukocyte Membrane Antigen, IgSF12.
Product # :
PRO-1618Price :
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Description
CD300A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (18-128) and having a molecular mass of 14.7kDa.CD300A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CD300A solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CD300A belongs to the CD300 family and contains 1 Ig-like V-type (immunoglobulin-like) domain. The protein is expressed not only by natural killer (NK) cells but also by T-cell subsets, B-cells, dendritic cells, mast cells, granulocytes and monocytes. CD300A is inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation.
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Synonyms
CD300a Molecule, CD300a Antigen, IRp60, CD300 Antigen-Like Family Member A, NK Inhibitory Receptor, Immunoglobulin Superfamily Member 12, CMRF35-Like Molecule 8, CMRF35-H, Inhibitory Receptor Protein 60, CMRF-35-H9, CMRF-35H, CLM-8, IRC1, IRC2, CMRF35H Leukocyte Immunoglobulin-Like Receptor, Leukocyte Membrane Antigen, IgSF12.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLSKCRTV AGPVGGSLSV QCPYEKEHRT LNKYWCRPPQ IFLCDKIVET KGSAGKRNGR VSIRDSPANL SFTVTLENLT EEDAGTYWCG VDTPWLRDFH DPVVEVEVSV FPAS
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.