Search results
595 results found for “Methylmalonic Aciduria”
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Name :
KLK8 MouseDescription:
Kallikrein-8 Mouse Recombinant
Ovasin, PRSS19, TADG14, NRPN, NP, Kallikrein 8 (Neuropsin/Ovasin) 2 EC 3.4.21.118, Kallikrein-8, Neuropsin, EC 3.4.21 61, HNP, HK8
Product # :
ENZ-1014Price :
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Shipped with Ice Packs
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Description
KLK8 Mouse Recombinant produced in Sf9 is a single, glycosylated polypeptide chain containing 240 amino acids (29-260) and having a molecular mass of 26.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). The KLK8 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK8 protein 0.5mg/ml is supplied in PBS, pH-7.4, and 10% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-8 is a serine protease which degrades various proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Kallikrein-8 takes part in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is essential for memory acquisition and synaptic plasticity. Kallikrein-8 participates in the secondary phase of pathogenesis following spinal cord injury and also takes part in skin desquamation and keratinocyte proliferation.
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Synonyms
Ovasin, PRSS19, TADG14, NRPN, NP, Kallikrein 8 (Neuropsin/Ovasin) 2 EC 3.4.21.118, Kallikrein-8, Neuropsin, EC 3.4.21 61, HNP, HK8
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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
QGSKILEGRE CIPHSQPWQA ALFQGERLIC GGVLVGDRWV LTAAHCKKQK YSVRLGDHSL QSRDQPEQEI QVAQSIQHPC YNNSNPEDHS HDIMLIRLQN SANLGDKVKP VQLANLCPKV GQKCIISGWG TVTSPQENFP NTLNCAEVKI YSQNKCERAY PGKITEGMVC AGSSNGADTC QGDSGGPLVC DGMLQGITSW GSDPCGKPEK PGVYTKICRY TTWIKKTMDN RDLEHHHHHH.
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 :
GDA Human, ActiveDescription:
Guanine Deaminase Human Recombinant, Active
Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.
Product # :
ENZ-982Price :
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Description
GDA Human Recombinant produced in E. coli is a single polypeptide chain containing 477 amino acids (1-454) and having a molecular mass of 53kDa.GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol, 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,000 pmol/min/ug, and is defined as the amount of enzyme that convert guanine to xanthine per minute at pH 8.0 at 37C.More Info
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Introduction
GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.
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Synonyms
Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.
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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 MGSMCAAQMP PLAHIFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE ASQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHASQ YSFAGSSIDL PLLEWLTKYT FPAEHRFQNI DFAEEVYTRV VRRTLKNGTT TACYFATIHT DSSLLLADIT DKFGQRAFVG KVCMDLNDTF PEYKETTEES IKETERFVSE MLQKNYSRVK PIVTPRFSLS CSETLMGELG NIAKTRDLHI QSHISENRDE VEAVKNLYPS YKNYTSVYDK NNLLTNKTVM AHGCYLSAEE LNVFHERGAS IAHCPNSNLS LSSGFLNVLE VLKHEVKIGL GTDVAGGYSY SMLDAIRRAV MVSNILLINK VNEKSLTLKE VFRLATLGGS QALGLDGEIG NFEVGKEFDA ILINPKASDS PIDLFYGDFF GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.
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 :
GLYAT HumanDescription:
Glycine-N-Acyltransferase Human Recombinant
Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.
Product # :
ENZ-148Price :
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Description
GLYAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 36.0 kDa.The GLYAT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLYAT protein (0.5mg/ml) is supplied in 20mM Tris-HCl, pH-8, 1mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GLYAT is a mitochondrial acyltransferase that conjugates glycine with acyl-CoA substrates in the mitochondria. GLYAT is vital to the detoxification of endogenous and xenobiotic acyl-CoA's.
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Synonyms
Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.
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Physical Appearance
GLYAT is supplied as a 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 MMLPLQGAQM LQMLEKSLRK SLPASLKVYG TVFHINHGNP FNLKAVVDKW PDFNTVVVCP QEQDMTDDLD HYTNTYQIYS KDPQNCQEFL GSPELINWKQ HLQIQSSQPS LNEAIQNLAA IKSFKVKQTQ RILYMAAETA KELTPFLLKS KILSPSGGKP KAINQEMFKL SSMDVTHAHL VNKFWHFGGN ERSQRFIERC IQTFPTCCLL GPEGTPVCWD LMDQTGEMRM AGTLPEYRLH GLVTYVIYSH AQKLGKLGFP VYSHVDYSNE AMQKMSYTLQ HVPIPRSWNQ WNCVPL.
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 :
CHST5 HumanDescription:
Carbohydrate Sulfotransferase 5 Human Recombinant
Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.
Product # :
ENZ-1165Price :
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Description
CHST5 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (27-395 a.a.) and having a molecular mass of 42.9kDa.CHST5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CHST5 protein solution (0.25mg/ml) containing 20% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is greater than 10,000 pmol/min/ug, and is defined as the amount of enzyme that sulfate from PAPS to Nacetyl-D-glucosamine per minute at pH 7.5, at 37˚C.
More Info
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Introduction
Carbohydrate Sulfotransferase 5 (CHST5) is a Golgi-embedded enzyme that is found in B cells, T cells and intestinal epithelium and is also mediates sulfation of keratan in cornea. CHST5 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine residues of keratan. CHST5 works on the non-reducing terminal GlcNAc of short andlong carbohydrate substrates that have poly-N-acetyllactosamine structures.
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Synonyms
Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.
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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
ADPEFSRQVP SSPAGLGERV HVLVLSSWRS GSSFVGQLFS QHPDVFYLME PAWHVWDTLS QGSAPALHMA VRDLIRSVFL CDMDVFDAYL PWRRNISDLF QWAVSRALCS PPVCEAFARG NISSEEVCKP LCATRPFGLA QEACSSYSHV VLKEVRFFNL QVLYPLLSDP ALNLRIVHLV RDPRAVLRSR EQTAKALARD NGIVLGTNGT WVEADPRLRV VNEVCRSHVR IAEAALHKPP PFLQDRYRLV RYEDLARDPL TVIRELYAFT GLGLTPQLQT WIHNITHGSG PGARREAFKT TSRDALSVSQ AWRHTLPFAK IRRVQELCGG ALQLLGYRSV HSELEQRDLS LDLLLPRGMD SFKWASSTEK QPESHHHHHH
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 :
C-JUN Human (241 a.a.)Description:
Jun Proto-Oncogene (1-241 a.a.) Human Recombinant
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
Product # :
PKA-001Price :
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Shipped with Ice Packs
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Description
C-JUN Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261 amino acids (1-241 a.a.) and having a molecular mass of 27.3kDa. The C-JUN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C-JUN solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.
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Synonyms
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
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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 MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP P.
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 :
CXCL8 Human (1-77)Description:
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-327Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton. The IL-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.sds-page
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin 8 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
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein has a total Mw of 8.9kDa.
What is the source or expression system of CXCL8 HUMAN (1-77) Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN (1-77) Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.
What is the amino acid sequence of CXCL8 HUMAN (1-77) Protein?
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
What applications can CXCL8 HUMAN (1-77) Protein be used in?
CXCL8 HUMAN (1-77) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN (1-77) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-77) 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.
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Name :
BCAT1 HumanDescription:
Branched Chain Amino-Acid Transaminase 1 Human Recombinant
Branched chain amino-acid transaminase 1 cytosolic, BCT1, BCATC, Protein ECA39, placental protein 18, PP18, PNAS121, MECA39, EC 2.6.1.42.
Product # :
ENZ-597Price :
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Shipped with Ice Packs
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Description
BCAT1 Recombinant produced in E. coli is a single polypeptide chain containing 409 amino acids (1-386) and having a molecular mass of 45.4kDa.BCAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The BCAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
BCAT1 catalyzes the leading reaction in the catabolism of the indispensable branched chain amino acids isoleucine, leucine and valine.
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Synonyms
Branched chain amino-acid transaminase 1 cytosolic, BCT1, BCATC, Protein ECA39, placental protein 18, PP18, PNAS121, MECA39, EC 2.6.1.42.
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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 MGSMKDCSNG CSAECTGEGG SKEVVGTFKA KDLIVTPATI LKEKPDPNNL VFGTVFTDHM LTVEWSSEFG WEKPHIKPLQ NLSLHPGSSA LHYAVELFEG LKAFRGVDNK IRLFQPNLNM DRMYRSAVRA TLPVFDKEEL LECIQQLVKL DQEWVPYSTS ASLYIRPTFI GTEPSLGVKK PTKALLFVLL SPVGPYFSSG TFNPVSLWAN PKYVRAWKGG TGDCKMGGNY GSSLFAQCEA VDNGCQQVLW LYGEDHQITE VGTMNLFLYW INEDGEEELA TPPLDGIILP GVTRRCILDL AHQWGEFKVS ERYLTMDDLT TALEGNRVRE MFGSGTACVV CPVSDILYKG ETIHIPTMEN GPKLASRILS KLTDIQYGRE ESDWTIVLS.
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 :
PPIH Human, HisDescription:
Cyclophilin-H Human Recombinant, His Tag
Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.
Product # :
ENZ-730Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-177) containing 186 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 20.3kDa (calculated).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in phosphate buffered saline pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.
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Synonyms
Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. PPIH is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASAVANSSPVNP VVFFDVSIGG QEVGRMKIEL FADVVPKTAE NFRQFCTGEF RKDGVPIGYK GSTFHRVIKD FMIQGGDFVN GDGTGVASIY RGPFADENFK LRHSAPGLLS MANSGPSTNG CQFFITCSKC DWLDGKHVVF GKIIDGLLVM RKIENVPTGP NNKPKLPVVI SQCGEM.
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 :
DBI MouseDescription:
Diazepam Binding Inhibitor Mouse Recombinant
Acyl-CoA-binding protein, ACBP, Diazepam-binding inhibitor, DBI, Endozepine, EP, Dbi.
Product # :
PRO-2527Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DBI Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87 a.a) and having a molecular mass of 12.4kDa. DBI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DBI protein solution (1mg/ml) contains Phosphate buffer saline (pH7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DBI, also known as Acyl-CoA-binding protein isoform 2, is a diazepam binding inhibitor, which is regulated by hormones. DBI participates in lipid metabolism and in the displacement of beta-carbolines & benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. Moreover, during adipocyte differentiation the expression of DBI is significantly induced. DBI preforms as an acyl-CoA pool former and regulates LCFA (long-chain fatty acids) metabolism in peripheral tissues.
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Synonyms
Acyl-CoA-binding protein, ACBP, Diazepam-binding inhibitor, DBI, Endozepine, EP, Dbi.
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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 MGSMSQAEFD KAAEEVKRLK TQPTDEEMLF IYSHFKQATV GDVNTDRPGL LDLKGKAKWD SWNKLKGTSK ESAMKTYVEK VDELKKKYGI
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 :
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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Shipped with Ice Packs
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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.
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.
- View Data Sheet
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 :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
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.
- View Data Sheet
Name :
IRF1 HumanDescription:
IFN Regulatory Factor-1 Human Recombinant
IRF-1, IRF1, MAR.
Product # :
CYT-449Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IRF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml in 20mM Tris pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
IRF1, IFN regulatory factor 1, is a member of the IFN regulatory transcription factor (IRF) family which regulates gene expression critical to immune response, hematopoiesis and proliferation. IRF-1 is a transcriptional activator for IFN-A, IFN-B, and IFN-G stimulated genes. IRF1 is also a tumor suppressor transcription factor inducing apoptosis of tumorigenic cell lines.
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Synonyms
IRF-1, IRF1, MAR.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Liquid IRF1 although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
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Background
What is the molecular weight/Mw of IRF1 HUMAN Protein?
IRF1 HUMAN Protein has a total Mw of XX15kDa.
What is the source or expression system of IRF1 HUMAN Protein?
Escherichia Coli.
What is the Purity of IRF1 HUMAN Protein?
IRF1 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IRF1 HUMAN Protein?
The biological functionality of IRF1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IRF1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
What applications can IRF1 HUMAN Protein be used in?
IRF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IRF1 HUMAN Protein?
The endotoxin level is minimal, IRF1 HUMAN 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 :
UBE2M HumanDescription:
Ubiquitin Conjugating Enzyme E2M Human Recombinant
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
Product # :
ENZ-345Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
UBE2M Human Recombinant produced E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.5kDa.UBE2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2M solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
UbcH12 is functional in in vitro NEDDylation reactions. It has been shown to form a thioester linkage with NEDD8 in the presence of the NEDD8 activating enzyme complex Uba3/APP-BP1. APP-BP1 binds to the amyloid precursor protein (APP) carboxy terminal domain and is important in conjunction with Uba3 and UbcH12 in driving cells through the S to M checkpoint. It was demonstrated to be the E2 responsible for the NEDDylation of the Cul-1 component of the SCF (?-TRCP) complex which is important as the E3-ligase in the ubiquitinylation of I?B?. NEDDylation of Cul-1 is essential for conjugation and processing of NF-?B p105 by SCF (?-TRCP) following phosphorylation of the complex. A dominant negative form of UbcH12, previously demonstrated to sequester NEDD8 and inhibit its conjugation, inhibits both conjugation and processing of p105, which is alleviated by wild-type UbcH12.
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Synonyms
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
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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 MGSHMIKLFS LKQQKKEEES AGGTKGSSKK ASAAQLRIQK DINELNLPKT CDISFSDPDD LLNFKLVICP DEGFYKSGKF VFSFKVGQGY PHDPPKVKCE TMVYHPNIDL EGNVCLNILR EDWKPVLTIN SIIYGLQYLF LEPNPEDPLN KEAAEVLQNN RRLFEQNVQR SMRGGYIGST YFERCLK
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 :
TGFB3 (207 a.a.) HumanDescription:
Transforming Growth Factor-Beta 3 (207 a.a.) Human Recombinant
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Product # :
CYT-319Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TGFB3 Human Recombinant protein encoding amino acids 644-850 and total molecular mass of 50 kDa (Including GST Tag).
Source
Escherichia Coli.
Formulation
100µl purified human TGF Beta 3protein at 100µg/ml in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol.
More Info
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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
TGF-beta 3 Human Recombinant although stable at 4°C for 1 week, should be stored at -20°C. 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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Applications
(a) ELISA.
(b) Western Blotting.
(c) Inhibition Assays.
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 :
CST3 Mouse, ActiveDescription:
Cystatin-C Mouse Recombinant, Active
Cystatin-C, Cystatin-3, Cst3, CST3
Product # :
PRO-2433Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 1.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25°C.
More Info
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Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
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Synonyms
Cystatin-C, Cystatin-3, Cst3, CST3
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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
ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA 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 :
Quantity :
Shipping Method :
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.
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.
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Name :
CXCL4 Variant 1 HumanDescription:
Platelet Factor-4 Variant 1 Human Recombinant
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL4 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
MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.
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 :
CD276 MouseDescription:
CD276 Mouse Recombinant
CD276 antigen, Cd276, 6030411F23Rik, AU016588, B7h3, B7RP-2, B7 homolog 3, B7-H3.
Product # :
PRO-2616Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD276 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 226 amino acids (29-248a.a.) and having a molecular mass of 24.7kDa. CD276 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD276 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CD276, belongs to the B7 family of immunoregulatory transmembrane glycoproteins expressed by T cells. CD276 is a costimulatory molecule for T cell activation in addition to IFN-gamma production. Furthermore, CD276 upregulates BRCC3 expression, preventing DNA defects caused by 5-Fu. CD276 is correlated with TNM stage of NSCLC and act as a potential biomarker for NSCLC-derived MPEs. CD276 inhibits natural-killer mediated cell lysis in tumor cells, and act as a marker for detection of neuroblastoma cells. CD276 is implicated in the development of acute as well as chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. In addition, CD276 provides the placenta & fetus a proper immunological environment during the course of pregnancy.
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Synonyms
CD276 antigen, Cd276, 6030411F23Rik, AU016588, B7h3, B7RP-2, B7 homolog 3, B7-H3.
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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
VEVQVSEDPV VALVDTDATL RCSFSPEPGF SLAQLNLIWQ LTDTKQLVHS FTEGRDQGSA
YSNRTALFPD LLVQGNASLR LQRVRVTDEG SYTCFVSIQD FDSAAVSLQV AAPYSKPSMT
LEPNKDLRPG NMVTITCSSY QGYPEAEVFW KDGQGVPLTG NVTTSQMANE RGLFDVHSVL
RVVLGANGTY SCLVRNPVLQ QDAHGSVTIT GQPLTFPPEA 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 :
ECI1 HumanDescription:
Enoyl-CoA Delta Isomerase 1 Human Recombinant
Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.
Product # :
ENZ-758Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ECI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (42-302 a.a.) and having a molecular mass of 31.1kDa. ECI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ECI1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Enoyl-CoA Delta Isomerase 1 (ECI1) is a main mitochondrial enzyme which takes part in beta-oxidation of unsaturated fatty acids. ECI1 is a member of the hydratase/isomerase superfamily. ECI1 catalyzes the transformation of 3-cis and 3-trans-enoyl-CoA esters to the 2-trans-enoylCoA intermediates.
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Synonyms
Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.
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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 MGSFGSQRVL VEPDAGAGVA VMKFKNPPVN SLSLEFLTEL VISLEKLEND KSFRGVILTS DRPGVFSAGL DLTEMCGRSP AHYAGYWKAV QELWLRLYQS NLVLVSAING ACPAGGCLVA LTCDYRILAD NPRYCIGLNE TQLGIIAPFW LKDTLENTIG HRAAERALQL GLLFPPAEAL QVGIVDQVVP EEQVQSTALS AIAQWMAIPD HARQLTKAMM RKATASRLVT QRDADVQNFV SFISKDSIQK SLQMYLERLK EEKG.
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 :
Osteocrin Human, HEKDescription:
Osteocrin Human Recombinant, HEK
Osteocrin, Musclin, OSTN.
Product # :
PRO-2818Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Osteocrin Human Recombinant is a single, glycosylated, polypeptide chain (28-133 a.a) containing a total of 112 amino acids and having a molecular mass of 12.5 kDa. Osteocrin is fused to a 6 a.a His-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The Osteocrin solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 20 ng/ml measured by its binding ability in a functional ELISA with Human NPRC.
More Info
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Synonyms
Osteocrin, Musclin, OSTN.
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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
VDVTTTEAFD SGVIDVQSTP TVREEKSATD LTAKLLLLDE LVSLENDVIE TKKKRSFSGF GSPLDRLSAG SVDHKGKQRK VVDHPKRRFG IPMDRIGRNR LSNSRGHHHH HH.
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Background
Research has demonstrated that osteocrin influences bone formation by enhancing the anabolic effects of osteoblasts, the cells responsible for new bone formation. In addition to its skeletal roles, osteocrin has been shown to regulate cardiovascular functions by modulating blood pressure and cardiac hypertrophy. Furthermore, emerging evidence suggests that osteocrin may play a role in the central nervous system, impacting cognitive function and neuroprotection.
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 :
CTRB1 HumanDescription:
Chymotrypsinogen-B1, Human Recombinant
Product # :
ENZ-1016Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
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Description
Recombinant Human CTRB1 expressed in E.coli containing 245 amino acids having a Mw of 27kDa is purified by standard chromatography techniques.
Source
E.coli
Formulation
The Human CTRB1 was lyophilized without any additives.
Purity
Greater than 95% as determined by HPLC.
Biological Activity
1100 units/mg protein.
One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmole of N-alpha-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 7.0 at 25°C.More Info
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Introduction
Chymotrypsinogen-B1 (CTRB1) belongs to the serine protease family of enzymes and forms a main precursor of the pancreatic proteolytic enzymes. CTRB1 is located next to a related chymotrypsinogen gene. CTRB1 is a protein coding gene which encodes different isoforms which may undergo similar processing to generate the mature protein.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Recombinant Human CTRB1 although stable at room temp for 1 week, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human CTRB1 in 1ml 50mM HAc which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPAGTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST SSPGVYARVTKLIPWVQKIL AAN.
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 :
MYD88 AntibodyDescription:
Myeloid Differentiation Primary Response 88, Mouse Anti Human
Myeloid differentiation primary response protein MyD88, MYD88, MYD88D.
Product # :
ANT-464Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.01% Sodium Azide.
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Introduction
Myeloid differentiation primary response gene 88 (MYD88) is a cytosolic adapter protein, which has a central role in the innate and adaptive immune response. MYD88 functions as a vital signal transducer in the interleukin-1 and Toll-like receptor signaling pathways. MYD88 acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. The MYD88 protein increases IL-8 transcription. MYD88 is involved in IL-18-mediated signaling pathway. MYD88 activates IRF1, resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. MYD88 is comprised of an N-terminal death domain and a C-terminal Toll-interleukin1 receptor domain. Patients with defects in the MYD88 gene have an increased susceptibility to pyogenic bacterial infections.
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Synonyms
Myeloid differentiation primary response protein MyD88, MYD88, MYD88D.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human MYD88 mAb, clone PAT22F11A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human MYD88 protein 1-309 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and Kappa light chain.
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Clone
PAT22F11A.
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Applications
The antibody has been tested by ELISA, 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 starting dilution is 1:1000.
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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
MYD88 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.
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Name :
SMAC/DIABLO AntibodyDescription:
SMAC/DIABLO, Mouse Anti Human
Diablo homolog mitochondrial, Second mitochondria-derived activator of caspase, Smac protein, Direct IAP-binding protein with low pI, DIABLO, SMAC, SMAC3, DIABLO-S, FLJ10537, FLJ25049.
Product # :
ANT-487Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Smac/Diablo is a proapoptotic protein that increases caspase activation in the cytochrome c/Apaf-1/caspase-9 pathway by its binding to the inhibitor of apoptosis proteins (IAPs) and removing their inhibitory activity. Smac/Diablo is a mitochondrial protein which enters the cytosol when cells go through apoptosis, and it moderates the caspase inhibition of IAPs.Smac/DIABLO expression is associated with the result of renal cell carcinoma.Dimeric form of Smac/DIABLO implies that once expressed in the cell the protein has a little probability of dissociation and, thus, loss of function. Survivin, Smac/DIABLO, & PKC-? play an important part in the inhibition of apoptosis by FGF-2 in human small cell lung cancer cells. Mitochondrial survivin associates with Smac/DIABLO, delaying its release. Decreased expression of Smac protein takes part in ovarian carcinogenesis and chemotherapeutic resistance. Smac/DIABLO plays a role in tumor cells during the pathway of apoptosis induction. SMAC protein is regulated by XIAP and degraded by proteasome. SMAC protein takes part inleukemic cell apoptosis. Smac is released during stress-induced apoptosis in multiple myeloma cells.
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Synonyms
Diablo homolog mitochondrial, Second mitochondria-derived activator of caspase, Smac protein, Direct IAP-binding protein with low pI, DIABLO, SMAC, SMAC3, DIABLO-S, FLJ10537, FLJ25049.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human SMAC/DIABLO mAb, clone PAT19F2A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human SMAC/DIABLO protein 56-239 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and Kappa light chain.
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Clone
PAT19F2A.
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Applications
The antibody has been tested by ELISA, 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 starting dilution is 1:3000.
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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
SMAC/DIABLO antibody was purified from mouse ascitic fluids by protein-A 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.
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Name :
CCNH AntibodyDescription:
Cyclin-H, Mouse Anti Human
CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.
Product # :
ANT-583Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.
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Synonyms
CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human CCNH mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CCNH amino acids 1-323 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT3G6AT.
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Applications
CCNH antibody has been tested by ELISA, 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 starting dilution for Western blot analysis is 1:1000.
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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
CCNH antibody was purified from mouse ascitic fluids by protein-A 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.