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1000 results found for “annexin”
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Name :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
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Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
Citations
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Rat Leptin Pegylated Quadruple Antagonist 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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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. 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.
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 :
METRN MouseDescription:
Meteorin Mouse Recombinant
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Product # :
PRO-2241Price :
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Shipped with Ice Packs
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Description
METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
METRN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
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Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
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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
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD 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 :
SERPINC1 Human, Sf9Description:
Serpin Peptidase Inhibitor, Clade C Member 1 Human Recombinant, Sf9
SERPINC1, AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1.
Product # :
PRO-2541Price :
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Description
SERPINC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (33-464a.a.) and having a molecular mass of 50.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). SERPINC is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SERPINC protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Serpin Peptidase Inhibitor, Clade C Member 1 (SERPINC1), which is a part of the serpin superfamily, is a plasma protease inhibitor. SERPINC1 inhibits thrombin and other activated serine proteases of the coagulation system, and regulates the blood coagulation cascade. SERPINC1 also inhibits Thrombin and Factors IXa, Xa and XIa. Deficiencies in SERPINC1 can cause ATIII deficiency, an autosomal dominant disease which might lead to a hereditary thrombophilia.
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Synonyms
SERPINC1, AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1.
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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
ADPHGSPVDI CTAKPRDIPM NPMCIYRSPE KKATEDEGSE QKIPEATNRR VWELSKANSR FATTFYQHLA DSKNDNDNIF LSPLSISTAF AMTKLGACND TLQQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SKLVSANRLF GDKSLTFNET YQDISELVYG AKLQPLDFKE NAEQSRAAIN KWVSNKTEGR ITDVIPSEAI NELTVLVLVN TIYFKGLWKS KFSPENTRKE LFYKADGESC SASMMYQEGK FRYRRVAEGT QVLELPFKGD DITMVLILPK PEKSLAKVEK ELTPEVLQEW LDELEEMMLV VHMPRFRIED GFSLKEQLQD MGLVDLFSPE KSKLPGIVAE GRDDLYVSDA FHKAFLEVNE EGSEAAASTA VVIAGRSLNP NRVTFKANRP FLVFIREVPL NTIIFMGRVA NPCVKHHHHH H.
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 :
EGLN3 HumanDescription:
Egl Nine Homolog 3 Human Recombinant
Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.
Product # :
PRO-1143Price :
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Shipped with Ice Packs
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Description
EGLN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 263 amino acids (1-239) and having a molecular mass of 29.8 kDa.EGLN3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EGLN3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 300mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.
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Synonyms
Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.
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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 MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED
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 :
EREG Human, HEKDescription:
Epiregulin Human Recombinant, HEK
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
Product # :
CYT-1206Price :
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Description
EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
Citations
More Info
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Introduction
"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."
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Synonyms
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
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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
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 32.6kDa.
What is the source or expression system of EREG Protein?
HEK293 cells.
What is the Purity of EREG Protein?
EREG Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
What is the amino acid sequence of EREG Protein?
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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 :
SPARC HumanDescription:
Secreted Protein Acidic & Rich in Cysteine Recombinant Human
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
Product # :
PRO-2602Price :
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Shipped at Room temp
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Description
Secreted Protein Acidic & Rich in Cysteine Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 32.7kDa.SPARC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is < 3.0 µg/mL, corresponding to a specific activity of > 333 IU/mg.
Citations
More Info
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Introduction
SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.
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Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secreted Protein Acidic & Rich in Cysteine 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 SPARC 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
APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI.
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 :
NHLH1 HumanDescription:
Nescient Helix Loop Helix 1 Human Recombinant
Nescient Helix Loop Helix 1, Class A Basic Helix-Loop-Helix Protein 35, Helix-Loop-Helix Protein 1, BHLHA35, NSCL1, HEN1.
Product # :
PRO-1547Price :
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Description
NHLH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-133) and having a molecular mass of 17.0kDa.NHLH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NHLH1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 40% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HLH (helix-loop-helix) proteins are a putative transcription factors family. Several HLH proteins take part in growth and development of an extensive range of tissues and species. NHLH1 functions as a DNA-binding protein and has a role in the regulation of cell-type determination in the developing nervous system.
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Synonyms
Nescient Helix Loop Helix 1, Class A Basic Helix-Loop-Helix Protein 35, Helix-Loop-Helix Protein 1, BHLHA35, NSCL1, HEN1.
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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 MGSMMLNSDT MELDLPPTHS ETESGFSDCG GGAGPDGAGP GGPGGGQARG PEPGEPGRKD LQHLSREERR RRRRATAKYR TAHATRERIR VEAFNLAFAE LRKLLPTLPP DKKLSKIEIL RLAICYISYL NHVLDV
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 :
AMH (452-560) HumanDescription:
Anti-Mullerian Hormone (452-560) Human Recombinant
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
Product # :
PRO-2843Price :
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Shipped at Room temp
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Description
Anti-Mullerian Hormone Human Recombinant produced in CHO is a Homodimer, glycosylated, polypeptide chain containing 109 amino acids (Ser452-Arg560) and having a total molecular mass of 23.4Da.
Anti-Mullerian Hormone is purified by proprietary chromatographic techniques.
Source
CHO Cells.
Formulation
AMH Lyophilized from a 0.2µm filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.
Purity
Greater than 97% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
Immobilized Recombinant Human AMH at 3 µg/mL (100 µL/well) will bind Recombinant Human MIS RII Fc Chimera with a linear range of 2.0-100 ng/mL. The activity was measured by its binding ability in a functional ELISA.Citations
More Info
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Introduction
Anti-Mullerian Hormone also known as AMH is a member of the TGF-beta family. AMH is a glycoprotein which is produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. AMH inhibits the growth of tumors derived from tissues of Muellerian duct origin. Moreover, AMH participates in Leydig cell differentiation and function in addition to follicular development in adult females.
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Synonyms
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
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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 reconstitute in sterile 4mM HCl to a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SAGATAADGP CALRELSVDL RAERSVLIPE TYQANNCQGV CGWPQSDRNP RYGNHVVLLL KMQVRGAALA RPPCCVPTAY AGKLLISLSE ERISAHHVPN MVATECGCR.
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 :
PODXL Human (335-387)Description:
Podocalyxin-Like (335-387 a.a) Human Recombinant
Product # :
PRO-2840Price :
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Shipped at Room temp
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Description
The PODXL Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The PODXL His-Tagged Fusion Protein, produced in E. coli, is a 11kDa protein containing 53 amino acid residues of the PODXL Human, 335-387 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized PODXLat -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
AGGASDEKLI SLICRAVKAT FNPAQDKCGI RLASVPGSQT VVVKEITIHS.
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Background
Podocalyxin-Like also known as PODXL is a glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein takes part in the regulation of both adhesion and cell morphology and cancer progression. PODXL plays a role as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. PODXL also functions as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligand which leads to rate increase of migration and cell-cell contacts in an integrin-dependent manner.
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 :
DCN Human, Sf9Description:
Decorin Human Recombinant, Sf9
Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.
Product # :
PRO-2232Price :
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 335 amino acids (31-359a.a.) and having a molecular mass of 37.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). DCN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.
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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
DEASGIGPEV PDDRDFEPSL GPVCPFRCQC HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKV SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKVTF NGLNQMIVIE LGTNPLKSSG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS LKGLNNLAKL GLSFNSISAV DNGSLANTPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYKH 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.
- View Data Sheet
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 :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
Citations
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.
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Name :
APOC1 HumanDescription:
Apolipoprotein C-I Human Recombinant
Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.
Product # :
CYT-812Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
APOC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids (27-83 a.a.) and having a molecular mass of 9.0kDa. APOC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
APOC1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
Apolipoprotein C-I (APOC1) which expressed mainly in the liver is a part of the apolipoprotein C family. APOC1 which is usually found in plasma and responsible for the activation of esterified lechitin cholesterol takes an important part in the exchange of esterified cholesterol among lipoproteins and in removal of cholesterol from tissues. APOC1 is activated when monocytes differentiate into macrophages. APOC1 protein’s main role is to inhibit CETP by altering the electric charge of HDL molecules. APOC1 is also binds free fatty acids and reduces their intracellular esterification.
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Synonyms
Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.
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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 MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.
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Background
Apolipoprotein C-I Human Recombinant: Unraveling the Complexity of Lipid Regulation
Abstract:
Apolipoprotein C-I (ApoC-I) is a remarkable protein that plays a significant role in lipid metabolism and cardiovascular health. It is primarily synthesized in the liver and is associated with lipoproteins involved in lipid transport. This research paper aims to provide a comprehensive overview of ApoC-I human recombinant, shedding light on its physiological functions, production methods, and potential therapeutic applications. By delving into the intricacies of ApoC-I, we can gain valuable insights into its role as a key player in lipid regulation and its potential as a therapeutic target.
Introduction:
The prevalence of lipid disorders and cardiovascular diseases necessitates a deeper understanding of the mechanisms governing lipid metabolism. ApoC-I, a critical component of lipoproteins, offers unique insights into the regulation of lipid levels and its implications for cardiovascular health.
Structure and Function of Apolipoprotein C-I:
ApoC-I exhibits a complex molecular structure, comprising functional domains that enable its interaction with lipoproteins. It plays a crucial role in regulating lipoprotein metabolism by inhibiting the activity of lipoprotein lipase and modulating the clearance of triglyceride-rich lipoproteins.
Regulation of Apolipoprotein C-I Expression:
The synthesis and secretion of ApoC-I are tightly regulated processes influenced by various factors, including nutritional status and hormonal signals. Understanding the regulatory mechanisms underlying ApoC-I expression can provide insights into its role in maintaining lipid homeostasis.
Apolipoprotein C-I and Cardiovascular Diseases:
Dysregulation of ApoC-I has been associated with various lipid disorders and cardiovascular diseases. Altered levels of ApoC-I have been observed in conditions such as hypertriglyceridemia and atherosclerosis, highlighting its potential as a biomarker for cardiovascular risk assessment.
Production of Apolipoprotein C-I Human Recombinant:
Recombinant ApoC-I can be produced using advanced biotechnological approaches, including recombinant DNA technology and protein expression systems. These methods enable large-scale production, purification, and characterization of ApoC-I, facilitating its potential therapeutic applications.
Therapeutic Potential of Apolipoprotein C-I Human Recombinant:
Targeting ApoC-I opens up exciting avenues for therapeutic interventions in lipid disorders and cardiovascular diseases. Modulating ApoC-I expression or function holds promise for restoring lipid balance and reducing the risk of cardiovascular complications.
Conclusion:
Apolipoprotein C-I human recombinant represents a fascinating area of research in the field of lipid metabolism and cardiovascular health. By unraveling the intricate interplay between ApoC-I, lipoproteins, and cardiovascular diseases, we can pave the way for novel therapeutic strategies and improved risk assessment. Further studies are required to fully understand the therapeutic potential of ApoC-I human recombinant and translate these findings into clinical applications.
What is the molecular weight/Mw of APOC1 Protein?
APOC1 Protein has a total Mw of 9kDa.
What is the source or expression system of APOC1 Protein?
Escherichia Coli.
What is the Purity of APOC1 Protein?
APOC1 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of APOC1 Protein?
The biological functionality of APOC1 Protein will be determined in the future.
What is the amino acid sequence of APOC1 Protein?
MGSSHHHHHH SSGLVPRGSH MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.
What applications can APOC1 Protein be used in?
APOC1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOC1 Protein?
The endotoxin level is minimal, APOC1 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 :
POMC HumanDescription:
Proopiomelanocortin Human Recombinant
Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.
Product # :
PRO-236Price :
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Shipped with Ice Packs
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Description
POMC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (27-267 a.a) and having a molecular mass of 28.9kDa (molecular weight on SDS-PAGE will appear higher).POMC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
POMC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 50% glycerol, 0.1mM PMSF, 0.1M Imidazole and 0.2M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Pro-opiomelanocortin preproprotein (POMC) is a polypeptide hormone precursor which experiences extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. POMC regulates the corticosteroid production in the adrenal cortex. Furthermore, POMC is cleaved into ten hormone chains named NPP, g-MSH, ACTH, a-MSH, CLIP, Lipotropin b, Lipotropin g, b-MSH,b endorphin and Met-enkephalin. POMC gene defects are the cause of POMC deficiency, which is characterized by red hair and adrenal insufficiency.
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Synonyms
Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.
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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 MWCLESSQCQ DLTTESNLLE CIRACKPDLS AETPMFPGNG DEQPLTENPR KYVMGHFRWD RFGRRNSSSS GSSGAGQKRE DVSAGEDCGP LPEGGPEPRS DGAKPGPREG KRSYSMEHFR WGKPVGKKRR PVKVYPNGAE DESAEAFPLE FKRELTGQRL
REGDGPDGPA DDGAGAQADL EHSLLVAAEK KDEGPYRMEH FRWGSPPKDK RYGGFMTSEK SQTPLVTLFK NAIIKNAYKK GE.
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 :
LYG2 HumanDescription:
Lysozyme G-Like 2 Human Recombinant
Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.
Product # :
PRO-1245Price :
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Description
LYG2 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (20-212) and having a molecular mass of 23.9 kDa. LYG2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The LYG2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
lysozyme G-like 2 and LYGH (LYG2), is a member of the glycosyl hydrolase 23 family. Lysozyme takes part in human innate immunity by causing bacterial cell lysis. LYG2 contains a SLT domain, a protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc).
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Synonyms
Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.
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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 MGSSYPFSHS MKPHLHPRLY HGCYGDIMTM KTSGATCDAN SVMNCGIRGS EMFAEMDLRA IKPYQTLIKE VGQRHCVDPA VIAAIISRES HGGSVLQDGW DHRGLKFGLM QLDKQTYHPV GAWDSKEHLS QATGILTERI KAIQKKFPTW SVAQHLKGGL SAFKSGIEAI ATPSDIDNDF VNDIIARAKF YKRQSF.
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 :
Visfatin AntibodyDescription:
Visfatin, Mouse Anti Human
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Product # :
ANT-368Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% glycerol & 0.02% Sodium Azide.
Citations
More Info
-
Introduction
Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-α, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It h
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Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
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Immunogen
Anti-human Visfatin mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Visfatin amino acids 1-491 purified from E. coli.
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Ig Subclass
Mouse IgG1heavy chain and κ light chain.
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Clone
P4D5AT.
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Applications
Visfatin 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.
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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
Visfatin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Transferrin Human, CHODescription:
Transferrin Human Recombinant, CHO
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Product # :
PRO-2782Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.
Source
Chinese Hamster Ovary cells.
Formulation
Transferrin solution contains 0.05% NaN3 and PBS.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
-
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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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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Applications
Immunoassay, cell culture.
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Background
Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.
The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.
The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.
The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.
By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.
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 :
CXCL17 RatDescription:
VEGF Co-regulated Chemokine 1 Rat Recombinant
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
Product # :
CHM-281Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.Citations
More Info
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Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
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Synonyms
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
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Background
What is the molecular weight/Mw of CXCL17 RAT Protein?
CXCL17 RAT Protein has a total Mw of 11.5kDa.
What is the source or expression system of CXCL17 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL17 RAT Protein?
CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL17 RAT Protein?
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.
What is the amino acid sequence of CXCL17 RAT Protein?
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
What applications can CXCL17 RAT Protein be used in?
CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL17 RAT Protein?
The endotoxin level is minimal, CXCL17 RAT Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL17 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL17 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PDCD6IP HumanDescription:
Programmed Cell Death 6 Interacting Protein Human Recombinant
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
Product # :
PRO-792Price :
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Description
PDCD6IP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 45.8 kDa. The PDCD6IP is fused to a 20 amino acid His-tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PDCD6IP is a Class E VPS protein which participates in concentration and sorting of cargo proteins of the multivesicular body or incorporation into intralumenal vesicles that are generated by invagination and scission from the limiting membrane of the endosome. PDCD6IP binds to the phospholipid lysobisphosphatidic acid which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. PDCD6IP is an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. PDCD6IP is mandatory for completion of cytokinesis. PDCD6IP takes part in HIV-1 virus budding. PDCD6IP replaces TSG101 in its function of supporting HIV-1 release. PDCD6IP takes part in the regulation of both apoptosis and cell proliferation. PDCD6IP is a cytoplasmic protein that cooperates with apoptosis-associated proteins (ALG-2 and PDCD6) and with the endocytosis-regulator CIN85. Overexpression of PDCD6IP and endophilin
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Synonyms
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
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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 MATFISVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RAAVGRPLDK HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK SCVLFNCAAL ASQIAAEQNL DNDEGLKIAA KHYQFASGAF LHIKETVLSA LSREPTVDIS PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE VFPVLAAKHC IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKTVASR YDEYVNVKDF SDKINRALAA AKKDNDFIYH DRVPDLKDLD PIGKATLVKS TPVNVPISQK FTDLFEKMVP VSVQQSLAAY NQRKADLVNR SIAQMREATT LA.
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 :
PDPN HumanDescription:
Podoplanin Human Recombinant
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
Product # :
PRO-626Price :
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Shipped with Ice Packs
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Description
PDPN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (99-207 a.a) and having a molecular mass of 13.4kDa. PDPN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl pH7.5 & 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors. -
Synonyms
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASTGQPEDD TETTGLEGGV AMPGAEDDVV TPGTSEDRYK SGLTTLVATS VNSVTGIRIE DLPTSESTVH AQEQSPSATA SNVATSHSTE KVDGDTQTTV EKDGLSTVTL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CA8 HumanDescription:
Carbonic Anhydrase 8 Human Recombinant
Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.
Product # :
ENZ-235Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CA8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-290) and having a molecular mass of 35.5kDa.CA8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CA8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CA8 was first called CA-related protein since there is a sequence similarity to other identified carbonic anhydrase genes. Still, this protein has no carbonic anhydrase activity - the reversible hydration of carbon dioxide. CA8 still holds a carbonic anhydrase designation due to obvious sequence similarity to other members of the carbonic anhydrase gene family. Mutations in CA8 result in cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3).
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Synonyms
Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.
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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 MGSHMADLSF IEDTVAFPEK EEDEEEEEEG VEWGYEEGVE WGLVFPDANG EYQSPINLNS REARYDPSLL DVRLSPNYVV CRDCEVTNDG HTIQVILKSK SVLSGGPLPQ GHEFELYEVR FHWGRENQRG SEHTVNFKAF PMELHLIHWN STLFGSIDEA VGKPHGIAII ALFVQIGKEH VGLKAVTEIL QDIQYKGKSK TIPCFNPNTL LPDPLLRDYW VYEGSLTIPP CSEGVTWILF RYPLTISQLQ IEEFRRLRTH VKGAELVEGC DGILGDNFRP TQPLSDRVIR AAFQ
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 :
TEK Mouse FcDescription:
TEK Tyrosine Kinase Endothelial Fc Chimera Mouse Recombinant
Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.
Product # :
PKA-249Price :
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Shipping Method :
Shipped at Room temp
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Description
Soluble TEK Mouse Recombinant fused with the Fc part of human IgG1 produced in CHO is a glycosylated disulfide-linked homodimer, polypeptide containing amino acids 119-740 amino acids and having a total molecular mass of 280 kDa. Mouse TIE-2/Fc monomer has a calculated molecular mass of approximately 105 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 140 kDa protein in SDS-PAGE under reducing conditions.The TEK Fc Chimera is purified by proprietary chromatographic techniques.
Source
CHO Cells.
Formulation
TEK Fc Chimera was lyophilized from a concentrated (1 mg/ml) sterile solution containing 1xPBS.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.
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Synonyms
Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized sTIE-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TEK 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 TIE-2 Fc Chimera in sterile water not less than 100µg/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 :
LAIR1 HumanDescription:
Leukocyte-Associated Ig-Like Receptor 1 Human Recombinant
Leukocyte-associated immunoglobulin-like receptor 1, LAIR-1, hLAIR1, CD305 antigen, LAIR1, CD305.
Product # :
PRO-431Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LAIR1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 105 and having a molecular mass of 11.5 kDa. The extracellular domain of LAIR-1 (22-125aa) was overexpressed in E.coli, and purified by using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl (pH7.5) 50mM NaCl and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
LAIR1 is a glycoprotein (~32kDa) expressed on the surface of the majority of human peripheral blood mononuclear leukocytes including T cells, B cells, NK cells, macrophages and dendritic cells. LAIR-1 functions as an inhibitory receptor in NK cells, T cells and B cells. Inhibitory receptors control the immune response to prevent lysis of cells recognized as self. Lair1 consists of a leader sequence, extracellular domain, transmembrane domain, cytoplasmic region.
LAIR1 is a member of both the immunoglobulin superfamily and the leukocyte-associated inhibitory receptor family. LAIR1 maps to a region of 19q13.4 labeled the leukocyte receptor cluster, which contains at least 29 genes encoding leukocyte-expressed receptors of the immunoglobulin superfamily. -
Synonyms
Leukocyte-associated immunoglobulin-like receptor 1, LAIR-1, hLAIR1, CD305 antigen, LAIR1, CD305.
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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
MQEEDLPRPS ISAEPGTVIP LGSHVTFVCR GPVGVQTFRL ERESRSTYND TEDVSQASPSESEARFRIDS VSEGNAGPYR CIYYKPPKWS EQSDYLELLV KETSG.
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 :
LOX HumanDescription:
Lysyl Oxidase Human Recombinant
Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.
Product # :
ENZ-829Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (169-417a.a) and having a molecular mass of 31.4kDa.LOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LOX protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lysyl Oxidase also known as LOX is an extracellular copper enzyme which initiates the crosslinking of collagens and elastin. LOX catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. Adding up to crosslinking extracellular matrix proteins, LOX plays a part in tumor suppression. Moreover, defects in LOX are the cause of autosomal recessive cutis laxa type I, CL type I. Two transcript variants encoding dissimilar isoforms have been found for LOX.
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Synonyms
Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.
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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 MGSDDPYNPY KYSDDNPYYN YYDTYERPRP GGRYRPGYGT GYFQYGLPDL VADPYYIQAS TYVQKMSMYN LRCAAEENCL ASTAYRADVR DYDHRVLLRF PQRVKNQGTS DFLPSRPRYS WEWHSCHQHY HSMDEFSHYD LLDANTQRRV AEGHKASFCL EDTSCDYGYH RRFACTAHTQ GLSPGCYDTY GADIDCQWID ITDVKPGNYI LKVSVNPSYL VPESDYTNNV VRCDIRYTGH HAYASGCTIS PY.
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 :
VAMP3 HumanDescription:
Synaptobrevin-3 Human Recombinant
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
Product # :
PRO-652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.
Source
Escherichia Coli.
Formulation
The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
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Synonyms
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
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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
MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.
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.