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1000 results found for “Retinol Binding Protein”
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Name :
IFIH1 HumanDescription:
Interferon Induced With Helicase C Domain 1 Human Recombinant
Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.
Product # :
PRO-1505Price :
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Description
IFIH1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 152,000 Dalton. IFIH1 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
IFIH1 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.
Purity
Greater than 93.0% as determined by SDS-PAGE.
More Info
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Introduction
IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.
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Synonyms
Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.
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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. Avoid multiple 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.
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Name :
DYNLRB2 HumanDescription:
Dynein Light Chain Roadblock-Type 2 Human Recombinant
Dynein light chain roadblock-type 2, Dynein light chain 2B cytoplasmic, Roadblock domain-containing protein 2, DYNLRB2, DNCL2B, DNLC2B, ROBLD2, MGC62033.
Product # :
PRO-174Price :
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Description
DYNLRB2 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 116 amino acids (1-96 a.a.) and having a molecular mass of 13kDa. The DYNLRB2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DYNLRB2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Dynein light chain roadblock-type 2 (DYNLRB2) functions as one of several non-catalytic accessory components of the cytoplasmic dynein complex which are considered to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein functions as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
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Synonyms
Dynein light chain roadblock-type 2, Dynein light chain 2B cytoplasmic, Roadblock domain-containing protein 2, DYNLRB2, DNCL2B, DNLC2B, ROBLD2, MGC62033.
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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 MAEVEETLKR IQSHKGVIGT MVVNAEGIPI RTTLDNSTTV QYAGLLHHLT MKAKSTVRDI DPQNDLTFLR IRSKKHEIMV APDKEYLLIV IQNPCE.
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 :
PITPNB HumanDescription:
Phosphatidylinositol Transfer Protein Beta Human Recombinant
Phosphatidylinositol transfer protein beta isoform, PI-TP-beta, PtdIns transfer protein beta, PtdInsTP beta, PITPNB, VIB1B, PtdInsTP.
Product # :
PRO-003Price :
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Description
PITPNB 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 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa. The PITPNB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PITPNB solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Phosphatidylinositol transfer protein beta isoform (PITPNB) is found in the cytoplasm, where it catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes. PITPNB mobilizes PI from the endoplasmic reticulum and regulates its release from stored vesicles in the Golgi network. PITPNB is extensively expressed in various tissues.
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Synonyms
Phosphatidylinositol transfer protein beta isoform, PI-TP-beta, PtdIns transfer protein beta, PtdInsTP beta, PITPNB, VIB1B, PtdInsTP.
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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 MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEK DGEKGQYTHK IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE LANSPDCPQM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNFHRQLFC WIDKWIDLTM EDIRRMEDET QKELETMRKR GSVRGTSAAD V.
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 :
LBH HumanDescription:
Limb Bud And Heart Development Human Recombinant
Protein LBH, hLBH, Limb Bud And Heart Development Homolog.
Product # :
PRO-423Price :
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Shipped with Ice Packs
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Description
LBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a) and having a molecular mass of 14.6kDa.LBH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LBH protein solution (0.25mg/ml) containing 20mM Tris-HCl(pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Limb Bud And Heart Development, (LBH) belongs to the LBH family.LBH is highly expressed in the heart, and expressed at low levels in placenta, lung, skeletal muscle, kidney and liver. In addition, LBH protein is a transcriptional activator which may act in mitogen-activated protein kinase signaling pathway. Among the diseases associated with LBH are celiac disease, and rheumatoid arthritis.
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Synonyms
Protein LBH, hLBH, Limb Bud And Heart Development Homolog.
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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 MGSMSIYFPI HCPDYLRSAK MTEVMMNTQP MEEIGLSPRK DGLSYQIFPD PSDFDRCCKL KDRLPSIVVE PTEGEVESGE LRWPPEEFLV QEDEQDNCEE TAKENKEQ
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 :
MINA HumanDescription:
MYC Induced Nuclear Antigen Human Recombinant
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
Product # :
PRO-2078Price :
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Description
MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MINA protein solution (0.25mg/ml) containing 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
MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.
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Synonyms
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
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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 MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.
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 :
ING2 HumanDescription:
Inhibitor of Growth Family, Member 2 Human Recombinant
Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.
Product # :
PRO-1739Price :
Quantity :
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Shipped with Ice Packs
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Description
ING2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 35.2kDa.ING2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ING2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).
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Synonyms
Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.
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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 MGSMLGQQQQ QLYSSAALLT GERSRLLTCY VQDYLECVES LPHDMQRNVS VLRELDNKYQ ETLKEIDDVY EKYKKEDDLN QKKRLQQLLQ RALINSQELG DEKIQIVTQM LELVENRARQ MELHSQCFQD PAESERASDK AKMDSSQPER SSRRPRRQRT SESRDLCHMA NGIEDCDDQP PKEKKSKSAK KKKRSKAKQE REASPVEFAI DPNEPTYCLC NQVSYGEMIG CDNEQCPIEW FHFSCVSLTY KPKGKWYCPK CRGDNEKTMD KSTEKTKKDR RSR.
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 :
P4HB MouseDescription:
Prolyl 4-Hydroxylase Beta Mouse Recombinant
Protein disulfide-isomerase, PDI, Cellular thyroid hormone-binding protein, Endoplasmic reticulum resident protein 59, ER protein 59, ERp59, Prolyl 4-hydroxylase subunit beta, p55.
Product # :
ENZ-935Price :
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Shipped with Ice Packs
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Description
P4HB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 498 amino acids (20-509a.a.) and having a molecular mass of 56.1kDa. P4HB is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
P4HB protein solution (0.5mg/ml) contains 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
P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.
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Synonyms
Protein disulfide-isomerase, PDI, Cellular thyroid hormone-binding protein, Endoplasmic reticulum resident protein 59, ER protein 59, ERp59, Prolyl 4-hydroxylase subunit beta, p55.
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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
DALEEEDNVL VLKKSNFEEA LAAHKYLLVE FYAPWCGHCK ALAPEYAKAA AKLKAEGSEI RLAKVDATEE SDLAQQYGVR GYPTIKFFKN GDTASPKEYT AGREADDIVN WLKKRTGPAA TTLSDTAAAE SLVDSSEVTV IGFFKDVESD SAKQFLLAAE AIDDIPFGIT SNSGVFSKYQ LDKDGVVLFK KFDEGRNNFE GEITKEKLLD FIKHNQLPLV IEFTEQTAPK IFGGEIKTHI LLFLPKSVSD YDGKLSSFKR AAEGFKGKIL FIFIDSDHTD NQRILEFFGL KKEECPAVRL ITLEEEMTKY KPESDELTAE KITEFCHRFL EGKIKPHLMS QEVPEDWDKQ PVKVLVGANF EEVAFDEKKN VFVEFYAPWC GHCKQLAPIW DKLGETYKDH ENIIIAKMDS TANEVEAVKV HSFPTLKFFP ASADRTVIDY NGERTLDGFK KFLESGGQDG AGDDEDLDLE EALEPDMEED DDQKAVKDEL LEHHHHHH.
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 :
CRYAB AntibodyDescription:
Crystallin Alpha B, Mouse Anti Human
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
ANT-306Price :
Quantity :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
Alpha crystallins are composed of two gene products; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of -crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human CRYAB mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CRYAB amino acids 1-175 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chains and κ light chain.
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Clone
P2E8AT.
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Applications
CRYAB 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 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.
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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
CRYAB 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 :
ACE2 (18-740) Human, BiotinDescription:
Angiotensin Converting Enzyme 2 (18-740 a.a.), Biotinylated Human Recombinant
Product # :
ENZ-1127Price :
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Description
The HEK293 derived ACE2 Human recombinant biotinylated protein contains the amino acids Gln 18-Ser 740 fused to His-AVI tag at C-terminal having a predicted Mw of 87.2 kDa ( migrates 95-125 kDa under reducing conditions on sds-page due to glycosilation). ACE2 Protein binds to SARS Coronavirus-2 [ CoV-2019 ] Spike receptor binding domain.
Source
HEK293 Cells
Formulation
ACE2 Human protein solution is supplied in 50mM Tris, pH7.5, 150mM NaCl and 20% glycerol.
Purity
ACE-2 Protein is >90% pure as determined SDS-PAGE.
Biological Activity
ACE2 activity was measured by its binding ability in a functional ELISA.
The immobilized Recombinant Human ACE2 protein binds to SARS CoV2 Spike protein Receptor Binding Domain at 2ug per ml.
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Introduction
ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
ACE-2 Human Recombinant Protein is shipped on ice packs. Upon arrival, Store at -20°C. The addition of 0.1% albmin is highly recommended for long term storage use.
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Purification Method
Purified by Protein-G chromatographic technique.
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 :
STAMBPL1 HumanDescription:
STAM Binding Protein Like 1 Human Recombinant
ALMalpha, AMSH-FP, AMSH-LP, bA399O19.2, AMSH-like protease, STAM Binding Protein Like 1, STAMBPL1, AMSHLP, KIAA1373.
Product # :
PRO-1354Price :
Quantity :
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Shipped with Ice Packs
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Description
STAMBPL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 458 amino acids (1-436) and having a molecular mass of 52 kDa. STAMBPL1 is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The STAMBPL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
STAM Binding Protein Like 1 (STAMBPL1) is a zinc metalloprotease which specifically cleaves 'Lys-63'-linked polyubiquitin chains, however, it doesn’t cleave 'Lys-48'-linked polyubiquitin chains. STAMBPL1 binds 2 zinc ions per subunit. The JAMM motif is vital for the protease activity. STAMBPL1 is a member of the peptidase M67C family. STAMBPL1 contains 1 MPN (JAB/Mov34) domain.
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Synonyms
ALMalpha, AMSH-FP, AMSH-LP, bA399O19.2, AMSH-like protease, STAM Binding Protein Like 1, STAMBPL1, AMSHLP, KIAA1373.
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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 SSGLVPRGSQ SHMDQPFTVN SLKKLAAMPD HTDVSLSPEE RVRALSKLGC NITISEDITP RRYFRSGVEM ERMASVYLEE GNLENAFVLY NKFITLFVEK LPNHRDYQQC AVPEKQDIMK KLKEIAFPRT DELKNDLLKK YNVEYQEYLQ SKNKYKAEIL KKLEHQRLIE AERKRIAQMR QQQLESEQFL FFEDQLKKQE LARGQMRSQQ TSGLSEQIDG SALSCFSTHQ NNSLLNVFAD QPNKSDATNY ASHSPPVNRA LTPAATLSAV QNLVVEGLRC VVLPEDLCHK FLQLAESNTV RGIETCGILC GKLTHNEFTI THVIVPKQSA GPDYCDMENV EELFNVQDQH DLLTLGWIHT HPTQTAFLSS VDLHTHCSYQ LMLPEAIAIV CSPKHKDTGI FRLTNAGMLE VSACKKKGFH PHTKEPRLFS ICKHVLVKDI KIIVLDLR.
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 :
HOXC11 HumanDescription:
Homeobox C11 Human Recombinant
800x600 Homeobox protein Hox-C11, Homeobox protein Hox-3H, HOXC11, HOX3H.
Product # :
PRO-1658Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
800x600 HOXC11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-304 a.a.) and having a molecular mass of 36.1kDa. HOXC11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HOXC11 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Homeobox C11 (HOXC11) is a member of the Abd-B homeobox family. The homeobox genes encode well conservedfamily of transcription factors that play a vital role in morphogenesis in all multicellular organisms. HOXC11is one of numerous homeobox HOXC genes placed in a cluster on chromosome 12. HOXC11 attaches to a promoterelement of the lactase-phlorizin hydrolase. HOXC11 also takes part in early intestinal development. An alternativelyspliced variant encoding a shorter isoform has been defined however, its full-length nature has not been determined.
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Synonyms
Homeobox protein Hox-C11, Homeobox protein Hox-3H, HOXC11, HOX3H.
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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 MGSMFNSVNL GNFCSPSRKE RGADFGERGS CASNLYLPSC TYYMPEFSTV SSFLPQAPSR QISYPYSAQV PPVREVSYGL EPSGKWHHRN SYSSCYAAAD ELMHRECLPP STVTEILMKN EGSYGGHHHP SAPHATPAGF YSSVNKNSVL PQAFDRFFDN AYCGGGDPPA EPPCSGKGEA KGEPEAPPAS GLASRAEAGA EAEAEEENTN PSSSGSAHSV AKEPAKGAAP NAPRTRKKRC PYSKFQIREL EREFFFNVYI NKEKRLQLSR MLNLTDRQVK IWFQNRRMKE KKLSRDRLQY FSGNPLL.
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 :
EFNA1 Human, HEKDescription:
Ephrin A1 Human Recombinant, HEK
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
Product # :
PRO-2477Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).
Source
HEK293 cells.
Formulation
EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
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Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
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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 one week 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. EFNA1 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
DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS 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 :
FURIN HumanDescription:
Furin Human Recombinant
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
Product # :
PRO-2199Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.
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Synonyms
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.
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 :
MRPL1 HumanDescription:
Mitochondrial Ribosomal Protein L1 Human Recombinant
BM022, L1MT, MRP-L1, 39S ribosomal protein L1, mitochondria, MRPL1.
Product # :
PRO-1431Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MRPL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (51-325) and having a molecular mass of 33.8kDa. MRPL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MRPL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Mitochondrial Ribosomal Protein L1 (MRPL1) exists as a component of the 39S ribosomal subunit and operates in conjunction with other MRPs to mediate protein synthesis. Mitochondrial ribosomes consist of a large 39S subunit and a small 28S subunit, both of which are consist of multiple mitochondrial ribosomal proteins (MRPs) that are encoded by nuclear genes and are vital for protein synthesis within mitochondria. MRPL1 exists as 2 isoforms produced by alternative splicing. Isoform 1 of MRPL1 is ubiquitously expressed while isoform 2 is particularly expressed in heart.
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Synonyms
BM022, L1MT, MRP-L1, 39S ribosomal protein L1, mitochondria, MRPL1.
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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 MGSKKTKKGA KEKTPDEKKD EIEKIKAYPY MEGEPEDDVY LKRLYPRQIY EVEKAVHLLK KFQILDFTSP KQSVYLDLTL DMALGKKKNV EPFTSVLSLP YPFASEINKV AVFTENASEV KIAEENGAAF AGGTSLIQKI WDDEIVADFY VAVPEIMPEL NRLRKKLNKK YPKLSRNSIG RDIPKMLELF KNGHEIKVDE ERENFLQTKI ATLDMSSDQI AANLQAVINE VCRHRPLNLG PFVVRAFLRS STSEGLLLKI DPLLPKEVKN EESEKEDA.
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 :
CST3 Protein, HisDescription:
Cystatin-C Human Recombinant, His Tag
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Product # :
PRO-656Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS PAGE.
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, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. 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
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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 :
BNP ProteinDescription:
B-type Natriuretic Peptide Human Recombinant
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-327Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Natriuretic Peptide Precursor B was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized B-type Natriuretic Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NPPB 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 B-type Natriuretic Peptide 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
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
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Background
What is the molecular weight / Mw of BNP Protein?
BNP Protein has a total Mw of 3.5kDa.
What is the source or expression system of BNP Protein?
Escherichia Coli.
What is the Purity of BNP Protein?
BNP Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BNP Protein?
The biological functionality of BNP Protein will be determined in the future.
What is the amino acid sequence of BNP Protein?
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
What applications can BNP Protein Protein be used in?
BNP Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BNP Protein?
The endotoxin level is minimal, BNP 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 :
C19ORF80 RatDescription:
Chromosome 19 Open Reading Frame 80 Rat Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-2024Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C19ORF80 Rat Recombinant produced in E. coli is a polypeptide chain containing 193 amino acids and having a total molecular mass of 22.0 kDa. C19ORF80 has a N-Terminal His-tag (10 AA residue).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from a 0.5mg/ml solution containing 0.03M Acetate buffer pH 4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
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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 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 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
MKHHHHHHAS VRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYKA TEARLTEAGR NLGLFDQALE FLGREVNQGR DATRELRTSL SEIQAEEDTL HLRAEATARS LREVARAQHA LRNSVRRLQV QLRGAWLGQA HQEFENLKDR ADKQNHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHMAA LPA
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 :
CDK5RAP3 HumanDescription:
CDK5 Regulatory Subunit Associated Protein 3 Human Recombinant
CDK5 Regulatory Subunit Associated Protein 3, LXXLL/Leucine-Zipper-Containing ARF-Binding Protein, LXXLL/Leucine-Zipper-Containing ARFbinding Protein, Ischemic Heart CDK5 Activator-Binding Protein C53, IC53, LZAP, CDK5 Regulatory Subunit Associated Protein IC53-2, CDK5 Regulatory Subunit-Associated Protein 3, CDK5 Activator-Binding Protein C53, Protein HSF-27, OK/SW-Cl.114, HSF-27, MST016, PP1553, C53, CDK5RAP3.
Product # :
PRO-2190Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDK5RAP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 526 amino acids (1-506 a.a) and having a molecular mass of 59kDa.CDK5RAP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDK5RAP3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CDK5 Regulatory Subunit Associated Protein 3 (CDK5RAP3) is a potential regulator of CDK5 activity via its interaction with CDK5R. Neuronal CDC2-like kinase, which is involved in the regulation of neuronal differentiation, is comprised of a catalytic subunit, CDK5, nad an activating subunit, p25NCK5A. CDK5RAP3 binds to p25NCK5A and hence may be involved in neuronal differentiation.
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Synonyms
CDK5 Regulatory Subunit Associated Protein 3, LXXLL/Leucine-Zipper-Containing ARF-Binding Protein, LXXLL/Leucine-Zipper-Containing ARFbinding Protein, Ischemic Heart CDK5 Activator-Binding Protein C53, IC53, LZAP, CDK5 Regulatory Subunit Associated Protein IC53-2, CDK5 Regulatory Subunit-Associated Protein 3, CDK5 Activator-Binding Protein C53, Protein HSF-27, OK/SW-Cl.114, HSF-27, MST016, PP1553, C53, CDK5RAP3.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MEDHQHVPID IQTSKLLDWL VDRRHCSLKW QSLVLTIREK INAAIQDMPE SEEIAQLLSG SYIHYFHCLR ILDLLKGTEA STKNIFGRYS SQRMKDWQEI IALYEKDNTY LVELSSLLVR NVNYEIPSLK KQIAKCQQLQ QEYSRKEEEC QAGAAEMREQ FYHSCKQYGI TGENVRGELL ALVKDLPSQL AEIGAAAQQS LGEAIDVYQA SVGFVCESPT EQVLPMLRFV QKRGNSTVYE WRTGTEPSVV ERPHLEELPE QVAEDAIDWG DFGVEAVSEG TDSGISAEAA GIDWGIFPES DSKDPGGDGI DWGDDAVALQ ITVLEAGTQA PEGVARGPDA LTLLEYTETR NQFLDELMEL EIFLAQRAVE LSEEADVLSV SQFQLAPAIL QGQTKEKMVT MVSVLEDLIG KLTSLQLQHL FMILASPRYV DRVTEFLQQK LKQSQLLALK KELMVQKQQE ALEEQAALEP KLDLLLEKTK ELQKLIEADI SKRYSGRPVN LMGTSL.
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 :
STIP1 HumanDescription:
Stress-Induced-Phosphoprotein 1 Human Recombinant
Stress Induced Phosphoprotein 1, Transformation-Sensitive Protein IEF SSP 3521, Renal Carcinoma Antigen NY-REN-11, Stress-Induced-Phosphoprotein 1, Hsp70/Hsp90-Organizing Protein, Hsc70/Hsp90-Organizing Protein, STI1, HOP, Epididymis Secretory Sperm Binding Protein Li 94n, NY-REN-11 Antigen, IEF-SSP-3521, HEL-S-94n, STI1L, P60.
Product # :
PRO-2334Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 543 amino acids (1-543 a.a) and having a molecular mass of 62.6kDa. STIP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STIP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.
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Synonyms
Stress Induced Phosphoprotein 1, Transformation-Sensitive Protein IEF SSP 3521, Renal Carcinoma Antigen NY-REN-11, Stress-Induced-Phosphoprotein 1, Hsp70/Hsp90-Organizing Protein, Hsc70/Hsp90-Organizing Protein, STI1, HOP, Epididymis Secretory Sperm Binding Protein Li 94n, NY-REN-11 Antigen, IEF-SSP-3521, HEL-S-94n, STI1L, P60.
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Physical Appearance
Sterile Filtered colorless solution.
-
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
MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLR NKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDK AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.
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 :
PAIP2 HumanDescription:
Polyadenylate-Binding Protein-Interacting protein 2 Human Recombinant
Poly(A) Binding Protein Interacting Protein 2, PABP- interacting protein 2, HSPC218, PAIP-2, PAIP2A, Polyadenylate-binding protein-interacting protein 2, PAIP2, MGC72018.
Product # :
PRO-748Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human PAIP2 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 147 amino acids (1-127 a.a.) and having a molecular mass of 17.1 kDa.PAIP2 human recombinant is fused to 20 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The PAIP2 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PAIP2 has a role as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. PAIP2 inhibitory activity on translation is mediated through its action on PABPC1. PAIP2 displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. PAIP2 association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization.
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Synonyms
Poly(A) Binding Protein Interacting Protein 2, PABP- interacting protein 2, HSPC218, PAIP-2, PAIP2A, Polyadenylate-binding protein-interacting protein 2, PAIP2, MGC72018.
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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 MKDPSRSSTS PSIINEDVII NGHSHEDDNP FAEYMWMENE EEFNRQIEEE LWEEEFIERC FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDGS SLEDLVVKSN LNPNAKEFVP GVKYGNI.
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 :
BAG1 HumanDescription:
BCL2-Associated Athanogene 1 Human Recombinant
BAG-1, Bcl-2-associated athanogene 1, RAP46, Bcl-2-binding protein, HAP.
Product # :
PRO-817Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
BAG1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 230 amino acids (1-230 a.a.) and having a molecular mass of 25.9 kDa. BAG1 protein is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
BAG1 Human solution containing 20mM Tris-HCl pH-7.5, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
BAG1 binds to BCL2 and is also called BCL2-associated athanogene. BAG1 increases the anti-apoptotic effects of BCL2 and is characterizes as a link between growth factor receptors and anti-apoptotic mechanisms. BAG1 inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG1 inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. BAG1 enhances the anti-cell death function of BCL2 induced by various stimuli.
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Synonyms
BAG-1, Bcl-2-associated athanogene 1, RAP46, Bcl-2-binding protein, HAP.
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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
MNRSQEVTRD EESTRSEEVT REEMAAAGLT VTVTHSNEKH DLHVTSQQGS SEPVVQDLAQ VVEEVIGVPQ SFQKLIFKGK SLKEMETPLS ALGIQDGCRV MLIGKKNSPQ EEVELKKLKH LEKSVEKIAD QLEELNKELT GIQQGFLPKD LQAEALCKLD RRVKATIEQF MKILEEIDTL ILPENFKDSR LKRKGLVKKV QAFLAECDTV EQNICQETER LQSTNFALAE.
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 :
Activin-A RatDescription:
Activin-A Rat Recombinant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-147Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/mlMore Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.
What is the source or expression system of Activin A Protein?
Ecoli
What is the Purity of Activin A Protein?
Activin A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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 :
Leptin-B TilapiaDescription:
Leptin-B Tilapia Recombinant
Product # :
CYT-1110Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
More Info
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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-B Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-B Tilapia 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 Leptin-B Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
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 :
GDF15 HumanDescription:
Growth and Differentiation Factor 15 Human Recombinant
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Product # :
CYT-335Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
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Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
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Background
What is the molecular weight/Mw of GDF15 HUMAN Protein?
GDF15 HUMAN Protein has a total Mw of 24.8kDa.
What is the source or expression system of GDF15 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF15 HUMAN Protein?
GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 HUMAN Protein?
The biological functionality of GDF15 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF15 HUMAN Protein?
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
What applications can GDF15 HUMAN Protein be used in?
GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 HUMAN Protein?
The endotoxin level is minimal, GDF15 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.