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1000 results found for “Dynactin”
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Name :
Calcitonin SalmonDescription:
Calcitonin Acetate Salmon
CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.
Product # :
HOR-262Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Calcitonin Acetate (Salmon) is a synthetic polypeptide of 32 amino acids in the same linear sequence that is found in calcitonin of salmon origin. The Molecular Formula is C145H240N44O48S2. Calcitonin Molecular Weight: 3431.9 Dalton.
Formulation
The calcitonin peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Calcitonin (CT) is a peptide hormone produced by the parafollicular cells of the thyroid gland in mammals and by the ultimobranchial gland of birds and fish. Salmon calcitonin (sCT), which is more potent and longer lasting than human CT, has been used widely for the treatment of osteoporosis, paget's disease, hypercalcemic shock and chronic pain in terminal cancer patients. sCT is one of the many bioactive peptides that require C-terminal amidation for full biological activity.
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Synonyms
CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Calcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CGRP 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 Calcitonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Calcitonin Acetate (Salmon) has an amino acid sequence of: Cys-Ser-Asn-Leu-Ser-Thr-Cys-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2.
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 :
GLUL Human, His ActiveDescription:
Glutamine Synthetase Human Recombinant, His Active
GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.
Product # :
ENZ-984Price :
Quantity :
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Shipped with Ice Packs
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Description
GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,800 pmol/min/ug, and is defined as the amount of enzyme that convert 1.0 pmole of L-glutamate to L-glutamine per miunte at pH 7.5 at 37C in coupled system with PK/LDH.More Info
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Introduction
GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.
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Synonyms
GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.
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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 MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.
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 :
IFNG Human, His ActiveDescription:
Interferon-gamma Human Recombinant, His Tag Active
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-1053Price :
Quantity :
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Shipped with Ice Packs
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Description
IFNG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (24-161 a.a) and having a molecular mass of 18.4kDa. IFNG is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IFNG protein solution (1mg/ml) containing Phosphate buffered saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cytotoxicity assay using WiDr cells. The ED50 for this effect is ≤ 5 ng/ml.
SDS-PAGE
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. -
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered colorless liquid.
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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 MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
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Background
What is the molecular weight/Mw of IFNG HUMAN, HIS ACTIVE Protein?
IFNG HUMAN, HIS ACTIVE Protein has a total Mw of 18.4kDa.
What is the source or expression system of IFNG HUMAN, HIS ACTIVE Protein?
Escherichia Coli.
What is the Purity of IFNG HUMAN, HIS ACTIVE Protein?
IFNG HUMAN, HIS ACTIVE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG HUMAN, HIS ACTIVE Protein?
Measured in a cytotoxicity assay using WiDr cells. The ED50 for this effect is ≤ 5 ng/ml.
What is the amino acid sequence of IFNG HUMAN, HIS ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
What applications can IFNG HUMAN, HIS ACTIVE Protein be used in?
IFNG HUMAN, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG HUMAN, HIS ACTIVE Protein?
The endotoxin level is minimal, IFNG HUMAN, HIS ACTIVE 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 :
CFD HumanDescription:
Complement Factor D Human
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
Product # :
PRO-2699Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Human Complement Factor D produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 24kDa.
Source
Human Plasma.
Formulation
CFD protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.
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Synonyms
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
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Physical Appearance
Sterile filtered solution.
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Stability
CFD Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
CSTB Human, ActiveDescription:
Cystatin-B, BioActive Human Recombinant
Cystatin-B, Stefin-B, Liver thiol proteinase inhibitor, CPI-B, CSTB, CST6, EPM1, PME, STFB
Product # :
PRO-2631Price :
Quantity :
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Shipped with Ice Packs
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Description
CSTB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-98 a.a.) and having a molecular mass of 13kDa.CSTB is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CSTB solution (1mg/1ml) contains 50mM NaCl and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 3.0nM. The inhibitory function of Cystatin B 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
Cystatin B or CSTB, is an protein (anti-protease) that is suspected to be involved in myoclonus epilepsy. As part of the encompasses proteins family, it has many cystatin-like sequences. Part of the cystatin superfamily are cysteine protease inhibitors; part don’t have the ability. CSTB can create a dimer that is stable because of noncovalent bonds and has a crucial part in shielding from lysosomal proteases leaking. Cystatin B can be found in the lysosomes, nucleus & the cytoplasm in cells.
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Synonyms
Cystatin-B, Stefin-B, Liver thiol proteinase inhibitor, CPI-B, CSTB, CST6, EPM1, PME, STFB
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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 MMCGAPSATQ PATAETQHIA DQVRSQLEEK ENKKFPVFKA VSFKSQVVAG TNYFIKVHVG DEDFVHLRVF QSLPHENKPL TLSNYQTNKA KHDELTYF
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 :
NME4 Human, ActiveDescription:
Non-Metastatic Cells 4 Human Recombinant, BioActive
Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.
Product # :
PRO-2642Price :
Quantity :
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Shipped with Ice Packs
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Description
NME4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa.NME4 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NME4 solution (0.5mg/ml) contains 40% glycerol, 20mM Tris-HCl buffer (pH 8.0) and 0.2M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 120unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.
More Info
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Introduction
Non-Metastatic Cells 4 or NME4, is a nucleoside diphosphate kinase located in the mitochondria, and is part of the NDK family of proteins. NME4 ais a very common enzyme that enhances transfer of gamma-phosphates, through a phosphohistidine as a intermediate, between dioxynucleoside tri- and diphosphates. NME4 is originated from the nm23 gene. NME4 has a crucial part in the creation of nucleoside triphosphates that are not ATP.
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Synonyms
Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.
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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 MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA
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 :
PGK2 Human, ActiveDescription:
Phosphoglycerate Kinase 2 Human Recombinant, BioActive
Phosphoglycerate kinase 2, dJ417L20.2, PGKB, PGKPSS, Phosphoglycerate kinase, testis specific
Product # :
PKA-125Price :
Quantity :
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Shipped with Ice Packs
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Description
PGK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-417a.a.) and having a molecular mass of 46.9kDa.PGK2 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGK2 solution (0.5mg/ml) contains 20% glycerol, 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity > 500unit/mg. One unit will convert 1 umole of 1,3-Bisphosphoglycerate to 3-PGA per minute at pH 8.0 at 37˚C.
More Info
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Introduction
PGK2, also known as Phosphoglycerate kinase 2, is a testis-specific form of phosphoglycerate kinase.Originally, it was assumed that PGK2was a pseudogene. However, nowadays it is known that this protein is a functional phosphoglycerate kinase. During the Embden-Meyerhof-Parnas pathway of glycolysis, in thelater stages of spermatogenesis, the protein catalyses the reversible conversion of 1, 3- bisphosphoglycerate to 3-phosphoglycerate.
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Synonyms
Phosphoglycerate kinase 2, dJ417L20.2, PGKB, PGKPSS, Phosphoglycerate kinase, testis specific
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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 MSLSKKLTLD KLDVRGKRVI MRVDFNVPMK KNQITNNQRI KASIPSIKYC LDNGAKAVVL MSHLGRPDGV PMPDKYSLAP VAVELKSLLG KDVLFLKDCV GAEVEKACAN PAPGSVILLE NLRFHVEEEG KGQDPSGKKI KAEPDKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPHKASGFLM KKELDYFAKA LENPVRPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM AYTFLKVLNN MEIGASLFDE EGAKIVKDIM AKAQKNGVRI TFPVDFVTGD KFDENAQVGK ATVASGISPG WMGLDCGPES NKNHAQVVAQ ARLIVWNGPL GVFEWDAFAK GTKALMDEIV KATSKGCITV IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM
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 :
MT IDescription:
Melanotan-I
Melanotan-I, MT-I, Melanotan-1.
Product # :
HOR-306Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Melanotan-I has the amino acid sequence of Ser-Tyr-Ser-Nle-Glu-His-D-Phe-Arg-Trp-Gly-Lys-Pro-Val and a molecular weight of 1647.4 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
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Synonyms
Melanotan-I, MT-I, Melanotan-1.
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Physical Appearance
Sterile Filtered off-White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Melanotan-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MT-I 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 Melanotan-I in sterile 1% acetic acid not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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 k9Description:
Cystatin-C Canine Recombinant
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Product # :
PRO-138Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cystatin-C Protein is a 14.85 kDa protein containing 133 amino acids fused to a 8 aa N-Terminal His-tag.
Source
E. coli
Formulation
K9 Cystatin-Cwas filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS, 50mM NaCl, pH 7.5.
Purity
Purity is greater than 95% as visualized 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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Stability
Store lyophilized Cystatin-C K9 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Cystatin-C 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 0.5 mg/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.
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Amino Acid Sequence
MKHHHHHHAS PGAGRRGSRP GAVGGAVDAD VGEEGVQQAL DFAVREYNRA SNDAYHSRAL RVLRARKQVV SGMNYFLEVE IGRTRCTKSQ PNLDNCPFHD QPHLMRKTLC SFQIYTVPWL GKTSLVKSSC QDV.
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 :
AFAP1 HumanDescription:
Actin Filament Associated Protein 1 Human Recombinant
Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 1.
Product # :
PRO-1972Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AFAP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 360 amino acids (250-588) and having a molecular mass of 39.2 kDa.AFAP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AFAP1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Actin Filament Associated Protein 1 (AFAP1) is a Src binding partner. AFAP1 is a possible modulator of actin filament integrity in response to cellular signals, and is also playing a role as an adaptor protein by connecting Src family members to actin filaments. AFAP1 takes partin the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.
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Synonyms
Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 1.
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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 MGCSGPVDSE CPPPPSSPVH KAELEKKLSS ERPSSDGEGV VENGITTCNG KEQVKRKKSS KSEAKGTVSK VTGKKITKII SLGKKKPSTD EQTSSAEEDV PTCGYLNVLS NSRWRERWCR VKDNKLIFHK DRTDLKTHIV SIPLRGCEVI PGLDCKHPLT FRLLRNGQEV AVLEASSSED MGRWIGILLA ETGSSTDPEA LHYDYIDVEM SASVIQTAKQ TFCFMNRRVI SANPYLGGTS NGYAHPSGTA LHYDDVPCIN GSLRGKKPPV ASNGVTGKGK TLSSQPKKAD PAAVVKRTGS NAAQYKYGKN RVEADAKRLQ TKEEELLKRK EALRNRLAQL.
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 :
DCPS HumanDescription:
Decapping Enzyme, Scavenger Human Recombinant
Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.
Product # :
ENZ-159Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCPS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337 a.a.) and having a molecular mass of 40.7kDa.DCPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCPS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Scavenger mRNA-decapping enzyme (DCPS) is a member of the HIT family. DCPS is required for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It was shown that DCPS hydrolyzes the residual m7GpppN cap structure after the complete 3'–5' degradation of the mRNA by the exosome. Furthermore, DCPS releases m7GMP and is incapable of cleaving cap structures attached to a long RNA chain.
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Synonyms
Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.
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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 MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS.
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 :
HMGA1 HumanDescription:
High Mobility Group AT-Hook 1 Human Recombinant
High mobility group protein HMG-I/HMG-Y, HMG-I(Y), High mobility group AT-hook protein 1, High mobility group protein A1, High mobility group protein R , HMGA1, HMGIY, HMG-R, HMGA1A.
Product # :
PRO-887Price :
Quantity :
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Description
HMGA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-107 a.a.) and having a molecular mass of 12.7kDa (Molecular weight on SDS-PAGE will appear higher).HMGA1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMGA1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.2M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
High mobility group protein HMG-I/HMG-Y (HMGA1) belongs to the non-histone chromosomal high mobility group protein (HMG) family. HMGA1 is composed of a highly conserved AT-hook DNA-binding domain which mediates binding to AT-rich sequences in the minor groove of chromosomal DNA. HMGA1 functions as an architectural chromatin-binding transcription factor modifying the conformation of DNA by modulating nuclear protein-DNA complexes. Furthermore, HMGA1 is involved in numerous cellular processes including growth regulation, viral induction of beta-IFN gene and regulation of inducible gene transcription.
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Synonyms
High mobility group protein HMG-I/HMG-Y, HMG-I(Y), High mobility group AT-hook protein 1, High mobility group protein A1, High mobility group protein R , HMGA1, HMGIY, HMG-R, HMGA1A.
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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
MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR PKGSKNKGAA KTRKTTTTPG RKPRGRPKKL EKEEEEGISQ ESSEEEQLEH HHHHH.
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 :
HPCAL1 HumanDescription:
Hippocalcin-Like 1 Human Recombinant
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3, VILIP-3
Product # :
PRO-254Price :
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Description
HPCAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213amino acids (1-193a.a.) and having a molecular wieght of 24.4kDa. The HPCAL1 is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HPCAL1 protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 1mM DTT 0.2M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.
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Synonyms
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3,
VILIP-3 -
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 MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF
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 :
SOST Human, HEKDescription:
Sclerostin Human Recombinant, HEK
Sclerostin, SOST, CDD, VBCH.
Product # :
PRO-2481Price :
Quantity :
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Shipped at Room temp
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Description
SOST Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-213) containing 196 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 22.4kDa (calculated).
Source
HEK293 Cells.
Formulation
SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
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Synonyms
Sclerostin, SOST, CDD, VBCH.
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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. SOST 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
QGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY 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.
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Name :
EIF1AY HumanDescription:
Eukaryotic Translation Initiation Factor 1A Y-linked Recombinant Human
Eukaryotic translation initiation factor 1A Y chromosome, Eukaryotic translation initiation factor 4C, eIF-4C, eIF-1A Y isoform.
Product # :
PRO-098Price :
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Description
EIF1AY produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-144.a.a) and having a molecular mass of 18.8kDa. EIF1AY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF1AY protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
EIF1AY is comparable to eukaryotic translation initiation factor 1A (EIF1A). EIF1AY protein is essential for highest rate of protein biosynthesis. EIF1AY increases ribosome dissociation into subunits and is obligatory for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5' end of capped RNA.
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Synonyms
Eukaryotic translation initiation factor 1A Y chromosome, Eukaryotic translation initiation factor 4C, eIF-4C, eIF-1A Y isoform.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPKNKGK GGKNRRRGKN ENESEKRELV FKEDGQEYAQ VIKMLGNGRL EALCFDGVKR LCHIRGKLRK KVWINTSDII LVGLRDYQDN KADVILKYNA DEARSLKAYG ELPEHAKINE TDTFGPGDDD EIQFDDIGDD DEDIDDI.
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 :
SPARC Human, Sf9Description:
Secreted Protein Acidic & Rich in Cysteine Human Recombinant, Sf9
SPARC, Basement-membrane protein 40, BM-40, Osteonectin, ON, Secreted protein acidic and rich in cysteine, OI17.
Product # :
PRO-2623Price :
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Description
SPARC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 295 amino acids (18-303 a.a) and having a molecular mass of 33.8kDa.SPARC is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPARC protein solution (0.5mg/ml) Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SPARC protein, or secreted protein acidic and rich in cysteine, or osteonectin or basement-membrane protein 40 is a protein that is coded by the SPARC gene in humans. It is a glycoprotein located in bones, that binds to calcium. The osteonectin is secreted from osteoblasts cells when boas are formed, mineralized and promotes the formation and creation of mineral crystals. Asides from calcium, it has been shown that this protein can also bind to collagen.
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Synonyms
SPARC, Basement-membrane protein 40, BM-40, Osteonectin, ON, Secreted protein acidic and rich in cysteine, OI17.
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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
ADPAPQQEAL PDETEVVEET VAEVTEVSVG ANPVQVEVGE FDDGAEETEE EVVAENPCQN
HHCKHGKVCE LDENNTPMCV CQDPTSCPAP IGEFEKVCSN DNKTFDSSCH FFATKCTLEG
TKKGHKLHLD YIGPCKYIPP CLDSELTEFP LRMRDWLKNV LVTLYERDED NNLLTEKQKL
RVKKIHENEK RLEAGDHPVE LLARDFEKNY NMYIFPVHWQ FGQLDQHPID GYLSHTELAP
LRAPLIPMEH CTTRFFETCD LDNDKYIALD EWAGCFGIKQ KDIDKDLVIH HHHHH
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 :
SPECC1 HumanDescription:
Sperm Antigen With Calponin Homology And Coiled-Coil 1 Human Recombinant
CYTSB, HCMOGT-1, HCMOGT1, NSP, Cytospin-B, Nuclear structure protein 5, NSP5, Sperm antigen HCMOGT-1, Sperm antigen with calponin homology and coiled-coil domains 1, SPECC1.
Product # :
PRO-2002Price :
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Description
SPECC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (458-761a.a) and having a molecular mass of 37.7kDa. SPECC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SPECC1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 1mM DTT and 0.1M NaCl.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Sperm Antigen With Calponin Homology And Coiled-Coil 1 (SPECC1) which is a part of the cytospin-A family takes part in cytokinesis and spindle organization. SPECC1 takes part in actin cytoskeleton organization and microtubule stabilization and therefore necessary for proper cell adhesion and migration.
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Synonyms
CYTSB, HCMOGT-1, HCMOGT1, NSP, Cytospin-B, Nuclear structure protein 5, NSP5, Sperm antigen HCMOGT-1, Sperm antigen with calponin homology and coiled-coil domains 1, SPECC1.
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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 MGSTQEGKII ELEQKCTGIL EQGRFEREKL LNIQQQLTCS LRKVEEENQG ALEMIKRLKE ENEKLNEFLE LERHNNNMMA KTLEECRVTL EGLKMENGSL KSHLQGEKQK ATEASAVEQT AESCEVQEML KVARAEKDLL ELSCNELRQE LLKANGEIKH VSSLLAKVEK DYSYLKEICD HQAEQLSRTS LKLQEKASES DAEIKDMKET IFELEDQVEQ HRAVKLHNNQ LISELESSVI KLEEQKSDLE RQLKTLTKQM KEETEEWRRF QADLQTAVVV ANDIKCEAQQ ELRTVKRKLL EEEEKNA.
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 :
PDCD6 HumanDescription:
Programmed Cell Death 6 Human Recombinant
Programmed cell death 6, ALG-2, PEF1B, Apoptosis-linked gene 2 protein, Probable calcium-binding protein ALG-2, FLJ46208, MGC111017, MGC119050, MGC9123.
Product # :
PRO-184Price :
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Description
PDCD6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-191a.a.) and having a molecular mass of 24.0 kDa. PDCD6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PDCD6 protein solution (0.5mg/1ml) is formulated in 10mM sodium citrate (pH 3.5) and 40% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PDCD6 is a calcium-binding protein and is a member of the penta-EF-hand protein family. Calcium binding is vital for homodimerization and for conformational changes essential for binding to other protein partners. PDCD6 takes part in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death. However, tests showed that in mice deficient for PDCD6, apoptosis was not blocked which suggests that PDCD6 is functionally redundant.
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Synonyms
Programmed cell death 6, ALG-2, PEF1B, Apoptosis-linked gene 2 protein, Probable calcium-binding protein ALG-2, FLJ46208, MGC111017, MGC119050, MGC9123.
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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 MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ ALSNGTWTPF NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR TYDRDNSGMI DKNELKQALS GFGYRLSDQF HDILIRKFDR QGRGQIAFDD FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY EQYLSMVFSI 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.
- View Data Sheet
Name :
HPSE ActiveDescription:
Recombinant Human Heparanase-1 Active
Product # :
ENZ-1032Price :
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Description
Heparanase Active Enzyme is produced in CHO cells.The protein is purified by several orthogonal chromatography steps.
Formulation
Heparanase Active Enzyme is supplied in20mM Acetate buffer and 750mM NaCl pH 5.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity of Heparanase Active Enzyme in-house standard is about 0.7 Units (1 unit = 1 μmole of reducing ends of heparan sulfate substrate formed per minute per mg Heparanase Active Enzyme at 37°C). The enzymatic activity of each Heparanase Active Enzyme batch is comparable to the standard as determined by activity assay in which immobilized heparan, released due to heparanase activity, is quantified colorimetrically. Recommended reaction buffer: 20 mM Citrate Phosphate buffer, pH 5.4; 50mM NaCl; 1mM CaCl2.
More Info
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Introduction
Heparanase is an endo β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).
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Data Sheet
To view the FULL VERSION data sheet click Heparanase-1 Active Enzyme
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Specificity
Heparanase Active Enzyme is identified by Western blot analysis with polyclonalrabbit anti-HPA1 antibodies as 2 subunits of 8-kDa and 50-kDa.
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Shipping Conditions
Heparanase Active Enzyme is shipped frozen on dry ice unless stated otherwise by the customer. Shipping fees to N. America and W. Europe is $400 Shipping fees to Asia, Australia and E. Europe is $500
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Storage Procedures
Store at –80ºC, avoid repeated 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 :
Resistin RatDescription:
Resistin Rat Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-1129Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.
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
Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Resistin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.
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 :
Leptin Mouse (D23L)Description:
Leptin D23L Mutant Mouse Recombinant
Product # :
CYT-1249Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin having a molecular mass of 16 kDa and was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Leptin Mouse is able to induce proliferation of BA/F3 cells stably transfected with the long form of human leptin receptor but its affinity toward this receptor was ~ 25-fold higher compared to non-mutated mouse leptin.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization Mouse Leptin can be stored at 4°C for 2-3 months. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Mouse in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids is Ala-Val-Pro-Ile-Gln
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Background
Leptin’s main part is to regulate long-term energy balance. Leptin produced mainly by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of different cells in the human body. The leptin receptor is found on various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value was calculated by DNA man program.
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 :
CST1 HumanDescription:
Cystatin SN Human Recombinant
Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.
Product # :
PRO-1006Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CST1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (21-141 a.a.) and having a molecular mass of 16.9kDa. CST1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CST1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Cystatin-SN (CST1) belongs to the type 2 salivary cystatin family found in a variety of fluids and secretions, including plasma, tears, and saliva. The cystatin superfamily includes proteins which contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, whereas others have lost or possibly never developed this inhibitory activity. CST1 is up-regulated in cancerous lesions of gastric cancer tissues compared to noncancerous regions, in addition clinicopathological analysis revealed a significant correlation between high expression of CST1.
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Synonyms
Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.
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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 MGSMWSPKEE DRIIPGGIYN ADLNDEWVQR ALHFAISEYN KATKDDYYRR PLRVLRARQQ TVGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WENRRSLVKS RCQES.
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 :
Adipsin HumanDescription:
Complement Factor D Human Recombinant
Complement factor D, EC 3.4.21.46, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD, ADN.
Product # :
PRO-1360Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Adipsin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (26-253 a.a) and having a molecular mass of 26.6kDa.Adipsin is fused to a 21 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
Adipsin protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.
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Synonyms
Complement factor D, EC 3.4.21.46, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD, ADN.
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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 MILGGREAEA HARPYMASVQ LNGAHLCGGV LVAEQWVLSA AHCLEDAADG KVQVLLGAHS LSQPEPSKRL YDVLRAVPHP DSQPDTIDHD LLLLQLSEKA TLGPAVRPLP WQRVDRDVAP GTLCDVAGWG IVNHAGRRPD SLQHVLLPVL DRATCNRRTH HDGAITERLM CAESNRRDSC KGDSGGPLVC GGVLEGVVTS GSRVCGNRKK PGIYTRVASY AAWIDSVLA.
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.