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1000 results found for “epiregulin”
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Name :
ARFIP2 HumanDescription:
ADP-Ribosylation Factor Interacting Protein 2 Human Recombinant
ADP-ribosylation factor interacting protein 2, partner of RAC1 (arfaptin 2), Partner of RAC1, Protein POR1, arfaptin-2, POR1.
Product # :
PRO-1201Price :
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Shipped with Ice Packs
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Description
ARFIP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 364 amino acids (1-341) and having a molecular mass of 40.2 kDa.ARFIP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ARFIP2 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Arfaptin 2 (ARFIP2) is a Rac1 binding protein essential for Rac-mediated actin polymerization and the succeeding formation of membrane ruffles and lamellipodia. ARFIP2 is a putative target protein of ADP-ribosylation factor. ARFIP2 is also involved in membrane ruffling. ARFIP2 expression is increased at sites of neurodegeneration. In addition, ARFIP2 interacts with the ADP ribosylation factor ARF6, a GTPase which associates with the plasma membrane and intracellular endosome vesicles, in a GTP dependent mode. Furthermore, Arfaptin 2 controls the aggregation of mutant Huntingtin protein by weakening proteasome function.
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Synonyms
ADP-ribosylation factor interacting protein 2, partner of RAC1 (arfaptin 2), Partner of RAC1, Protein POR1, arfaptin-2, POR1.
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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 MGS TDGILG KAATMEIPIH GNGEARQLPE DDGLEQDLQQ VMVSGPNLNE TSIVSGGYGG SGDGLIPTGS GRHPSHSTTP SGPGDEVARG IAGEKFDIVK KWGINTYKCT KQLLSERFGR GSRTVDLELE LQIELLRETK RKYESVLQLG RALTAHLYSL LQTQHALGDA FADLSQKSPE LQEEFGYNAE TQKLLCKNGE TLLGAVNFFV SSINTLVTKT MEDTLMTVKQ YEAARLEYDA YRTDLEELSL GPRDAGTRGR LESAQATFQA HRDKYEKLRG DVAIKLKFLE ENKIKVMHKQ LLLFHNAVSA YFAGNQKQLE QTLQQFNIKL RPPGAEKPSW LEEQ
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 :
Eotaxin HumanDescription:
Eotaxin Human Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Product # :
CHM-256Price :
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Description
Eotaxin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8345.9 Dalton. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.Citations
More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin Human Recombinant 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
GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
SMKYLDQKSP TPKP.
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Background
What is the molecular weight/Mw of EOTAXIN HUMAN Protein?
EOTAXIN HUMAN Protein has a total Mw of 8.3459kDa.
What is the source or expression system of EOTAXIN HUMAN Protein?
Escherichia Coli.
What is the Purity of EOTAXIN HUMAN Protein?
EOTAXIN HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN HUMAN Protein?
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.
What is the amino acid sequence of EOTAXIN HUMAN Protein?
GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
SMKYLDQKSP TPKP.
What applications can EOTAXIN HUMAN Protein be used in?
EOTAXIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN HUMAN Protein?
The endotoxin level is minimal, EOTAXIN HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant EOTAXIN HUMAN 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 EOTAXIN HUMAN?
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.
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Name :
TAGLN3 HumanDescription:
Transgelin-3 Human Recombinant
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
Product # :
PRO-946Price :
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Shipped with Ice Packs
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Description
TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TAGLN3 solution (0.5mg/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
TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.
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Synonyms
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
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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 MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM
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 :
PFN1 HumanDescription:
Profilin-1 Human Recombinant
Profilin-1, Profilin I, PFN1.
Product # :
PRO-528Price :
Quantity :
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Shipped with Ice Packs
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Description
PFN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 15kDa.The PFN1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFN1 protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.
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Synonyms
Profilin-1, Profilin I, PFN1.
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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
MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN VTVTKTDKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY.
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 :
CAPZA2 HumanDescription:
Capping Protein (Actin Filament) Muscle Z-Line Alpha 2 Human Recombinant
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
Product # :
PRO-1721Price :
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Shipped with Ice Packs
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Description
CAPZA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-286 a.a) and having a molecular mass of 35.3kDa.CAPZA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAPZA2 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.
Citations
More Info
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Introduction
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.
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Synonyms
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
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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 MGSMADLEEQ LSDEEKVRIA AKFIIHAPPG EFNEVFNDVR LLLNNDNLLR EGAAHAFAQY NLDQFTPVKI EGYEDQVLIT EHGDLGNGKF LDPKNRICFK FDHLRKEATD PRPCEVENAV ESWRTSVETA LRAYVKEHYP NGVCTVYGKK IDGQQTIIAC IESHQFQAKN FWNGRWRSEW KFTITPSTTQ VVGILKIQVH YYEDGNVQLV SHKDIQDSLT VSNEVQTAKE FIKIVEAAEN EYQTAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA.
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 :
Pleiotrophin HumanDescription:
Pleiotrophin Human Recombinant
PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.
Product # :
CYT-749Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pleiotrophin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.3kDa.The Pleiotrophin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Pleiotrophin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.sds-page
Citations
More Info
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Introduction
Pleiotrophin (Osteoblast-Specific Factor-1, OSF-1) contains 136 amino acid residues. The sequence is very rich in cationic amino acids (24% of the residues); lysine cluster sequences are found in the N-terminal and C-terminal ends of the structure.
The OSF-1 gene was shown by Northern blotting analysis to be expressed in mouse calvarial osteoblast-enriched cells and in mouse brain tissues, but not in thymus, spleen, kidney, liver, lung, testis or heart. Pleiotrophin has the ability to promote adhesion, migration, expansion, and differentiation of human osteoprogenitor cells. In addition to certain types of cancer, the embryonic growth and differentiation factor pleiotrophin is found also in adults in inflammatory diseases. In osteoarthritis, pleiotrophin is especially expressed in early stages, and its concentrations in the synovial fluid could serve as a marker for the progress of the disease. Pleitrophin might be involved in cartilage repair in osteoarthritis, in particular, in earlier stages. -
Synonyms
PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pleiotrophin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pleiotrophin 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 Pleiotrophin 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
GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD.
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 :
Globular Adiponectin HumanDescription:
Globular Adiponectin Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-615Price :
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Shipped at Room temp
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Description
gAcrp30 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 145 amino acids and having a molecular mass of 16.7kDa. The gAcrp30 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Sterile filtered and lyophilized from 10mM sodium phosphate & 0.5mM DTT, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.
Citations
More Info
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Introduction
gAcrp30 globular protein, exists as a result of proteolytic processing of adiponectin. Adiponectin is manufactured and secreted solely by adipocytes, and is a highly obtained plasma protein, accounting for up to 0.05% of total serum protein. Similar to Adiponectin, gAcrp30 is able of lowering hyperglycemia and reversing INS resistance. In addition, gAcrp30 is an significant protein that is involved in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids. AdipoR1 & AdipoR2 are the 2 signaling receptors for adiponectin and gAcrp30 that were recently been identified.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Stability
For long term, 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 two weeks.
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Solubility
We recommended reconstituting gAcrp30 at a concentration of 0.1mg per ml with 10mM sodium phosphate & 0.5mM DTT, pH 7.5. which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.
What is the amino acid sequence of ADIPONECTIN Protein?
MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
KLRC3 HumanDescription:
Killer Cell Lectin-Like Receptor Subfamily C, Member 3 Human Recombinant
Killer Cell Lectin-Like Receptor Subfamily C Member 3, NK Cell Receptor E, NKG2-E Type II Integral Membrane Protein, NKG2-E-Activating NK Receptor, NKG2E.
Product # :
PRO-1230Price :
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Shipped with Ice Packs
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Description
KLRC3 Human Recombinant produced in E. coli is a single polypeptide chain containing 171 amino acids (94-240) and having a molecular mass of 19.0 kDa.KLRC3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The KLRC3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
KLRC3 belongs to the NKG2 group that can be found mostly in natural killer (NK) cells and encodes a family of transmembrane proteins known for their C-type lectin domain and their type II membrane orientation (extracellular C terminus). The NKG2 gene family is situated inside the NK complex, a region which has quite a few C-type lectin genes mostly expressed on NK cells.
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Synonyms
Killer Cell Lectin-Like Receptor Subfamily C Member 3, NK Cell Receptor E, NKG2-E Type II Integral Membrane Protein, NKG2-E-Activating NK Receptor, NKG2E.
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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 MGSMIPFLEQ NNSSPNTRTQ KARPCGHCPE EWITYSNSCY YIGKERRTWE ESLQACASKN SSSLLSIDNE EEMKFLASIL PSSWIGVFRN SSHHPWVTIN GLAFKHEIKD SDHAERNCAM LHVRGLISDQ CGSSRIIRRG FIMLTRLVLN S
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 :
KRT5 HumanDescription:
Cytokeratin 5 Human Recombinant
Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.
Product # :
PRO-1940Price :
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Shipped with Ice Packs
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Description
KRT5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 613 amino acids (1-590) and having a molecular mass of 64.8 kDa.KRT5 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The KRT5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cytokeratin 5 (KRT5) belongs to the keratin gene family. The type II cytokeratins are comprised of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed throughout differentiation of simple and stratified epithelial tissues. The type II cytokeratins are clustered in a region of chromosome 12q12-q13. The KRT5 type II cytokeratin is specifically expressed in the basal layer of the epidermis with family member KRT14. Mutations in these genes are linked with a complex of diseases termed epidermolysis bullosa simplex.
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Synonyms
Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSRQSSV SFRSGGSRSF STASAITPSV SRTSFTSVSR SGGGGGGGFG RVSLAGACGV GGYGSRSLYN LGGSKRISIS TSGGSFRNRF GAGAGGGYGF GGGAGSGFGF GGGAGGGFGL GGGAGFGGGF GGPGFPVCPP GGIQEVTVNQ SLLTPLNLQI DPSIQRVRTE EREQIKTLNN KFASFIDKVR FLEQQNKVLD TKWTLLQEQG TKTVRQNLEP LFEQYINNLR RQLDSIVGER GRLDSELRNM QDLVEDFKNK YEDEINKRTT AENEFVMLKK DVDAAYMNKV ELEAKVDALM DEINFMKMFF DAELSQMQTH VSDTSVVLSM DNNRNLDLDS IIAEVKAQYE EIANRSRTEA ESWYQTKYEE LQQTAGRHGD DLRNTKHEIS EMNRMIQRLR AEIDNVKKQC ANLQNAIADA EQRGELALKD ARNKLAELEE ALQKAKQDMA RLLREYQELM NTKLALDVEI ATYRKLLEGE ECRLSGEGVG PVNISVVTSS VSSGYGSGSG YGGGLGGGLG GGLGGGLAGG GSGSYYSSSS GGVGLSGGLS VGGSGFSASS GRGLGVGFGS GGGSSSSVKF VSTTSSSRKS FKS.
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 :
CCL4L1 HumanDescription:
LAG-1 Human Recombinant (CCL4L1)
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
Product # :
CHM-018Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LAG-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa.The CCL4L1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAG-1 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.Citations
More Info
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Introduction
CCL4L1 (C-C motif chemokine 4-like) is a member of to intercrine beta (chemokine CC) family. The CCL4L1 protein is similar to CCL4 which inhibits HIV replication in peripheral blood monocytes which express CCR5.
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Synonyms
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LAG-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4L1 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 LAG-1 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
APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN.
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Background
What is the molecular weight/Mw of CCL4L1 HUMAN Protein?
CCL4L1 HUMAN Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL4L1 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL4L1 HUMAN Protein?
CCL4L1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL4L1 HUMAN Protein?
The ED50 as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.
What is the amino acid sequence of CCL4L1 HUMAN Protein?
APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN.
What applications can CCL4L1 HUMAN Protein be used in?
CCL4L1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL4L1 HUMAN Protein?
The endotoxin level is minimal, CCL4L1 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL4L1 HUMAN 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 CCL4L1 HUMAN?
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 :
CDC26 HumanDescription:
Cell Division Cycle 26 Human Recombinant
Anaphase-promoting complex subunit CDC26, Anaphase-promoting complex subunit 12, APC12, Cell division cycle protein 26 homolog, CDC26, ANAPC12, C9orf17.
Product # :
PRO-241Price :
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Shipping Method :
Shipped with Ice Packs
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Description
CDC26 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a) and having a molecular mass of 11.9kDa.CDC26 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDC26 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
CDC26 is a member of the CDC26 family which arranges progression via mitosis by enhancing cell-cycle regulators with ubiquitin chains. CDC26 is a component of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated E3 ubiquitin ligase which directs progression through mitosis and the G1 phase of the cell cycle. The APC/C complex operates by mediating ubiquitination and subsequent degradation of target proteins.
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Synonyms
Anaphase-promoting complex subunit CDC26, Anaphase-promoting complex subunit 12, APC12, Cell division cycle protein 26 homolog, CDC26, ANAPC12, C9orf17.
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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 MLRRKPTRLE LKLDDIEEFE NIRKDLETRK KQKEDVEVVG GSDGEGAIGL SSDPKSREQM INDRIGYKPQ PKPNNRSSQF GSLEF.
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 tA MouseDescription:
Leptin Antagonist Triple Mutant Mouse Recombinant
Product # :
CYT-354Price :
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Description
Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting Leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant 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 Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted 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 was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
RLN2 HumanDescription:
Relaxin-2 Human Recombinant
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
Product # :
PRO-1327Price :
Quantity :
Shipping Method :
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Description
RLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (25-185 a.a) and having a molecular mass of 20.7kDa.RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RLN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
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Synonyms
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
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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 MGSDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFC.
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 :
TriptorelinDescription:
Triptorelin Acetate
Product # :
HOR-238Price :
Quantity :
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Shipped at Room temp
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Description
Triptorelin C64H82N18O13, Pyr-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-Gly-NH2 is a synthetic analogue of gonadorelin (GnRH). As a result of the substitution of the 6th amino acid residue in the native molecule, the agonistic effect is more pronounced and the plasma half-life prolonged.
Formulation
The protein (1 mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Trp although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Trp 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 Trp 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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Background
What is the Purity of TRIPTORELIN Protein?
TRIPTORELIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of TRIPTORELIN Protein?
The biological functionality of TRIPTORELIN Protein will be determined in the future.
What applications can TRIPTORELIN Protein be used in?
TRIPTORELIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TRIPTORELIN Protein?
The endotoxin level is minimal, TRIPTORELIN 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 :
ITGB3BP HumanDescription:
Integrin Beta 3 Binding Protein Human Recombinant
CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.
Product # :
PRO-1435Price :
Quantity :
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Shipped with Ice Packs
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Description
ITGB3BP Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 27.1kDa. ITGB3BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ITGB3BP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.
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Synonyms
CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.
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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 MGSMPFAPVA QARVQWHDFR SLQHLLPAFK RFSCLSLGSS WDYSVKRSLK LDGLLEENSF DPSKITRKKS VITYSPTTGT CQMSLFASPT SSEEQKHRNG LSNEKRKKLN HPSLTESKES TTKDNDEFMM LLSKVEKLSE EIMEIMQNLS SIQALEGSRE LENLIGISCA SHFLKREMQK TKELMTKVNK QKLFEKSTGL PHKASRHLDS YEFLKAILN.
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 :
EPHX1 AntibodyDescription:
Epoxide hydrolase 1, Mouse Anti Human
Epoxide hydrolase 1, Microsomal epoxide hydrolase, Epoxide hydratase, EPHX1, EPHX, EPOX, MEH.
Product # :
ANT-440Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
-
Introduction
Epoxide hydrolase is a vital biotransformation enzyme which converts epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase functions in both the activation and detoxification of epoxides. Mutations in the EPHX1 gene cause preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.
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Synonyms
Epoxide hydrolase 1, Microsomal epoxide hydrolase, Epoxide hydratase, EPHX1, EPHX, EPOX, MEH.
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Immunogen
Anti-human EPHX1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EPHX1 amino acids 21-455 purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
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Clone
PAT2E5AT.
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Applications
EPHX1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1000 ~ 2000. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
EPHX1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EGF Long HumanDescription:
Epidermal Growth Factor Long Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-798Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.Citations
More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long 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 EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
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Background
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 12.3kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.
What is the amino acid sequence of EGF Protein?
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF 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 :
SERPINA5 Human, ActiveDescription:
Serpin Peptidase Inhibitor, Clade A Member 5 Human Recombinant, Active
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
Product # :
PRO-2523Price :
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Shipped with Ice Packs
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Description
SERPINA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (20-406 a.a) and having a molecular mass of 45.9kDa.SERPINA5 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SERPINA5 protein solution (0.5mg/ml) contains 150mM NaCl, 10% glycerol & 20 mM MES buffer (pH6.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit Thrombin cleavage of substrate Boc-VPR-AMC. The IC50 for this effect is less or equal to 2 nM.
Citations
More Info
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Introduction
SERPINA5 up regulates TAFI activation by inhibiting the protein C activation. SERPINA5 is a significant regulator in the equilibrium between coagulation and fibrinolysis by differentially inhibiting the activation of TAFI and of Protein-C. SERPINA5 belongs to the serpin serine proteinase inhibitor family. SERPINA5 protein inhibits plasminogen activators as well as activated protein C.
SERPINA5 is secreted in plasma & liver. SERPINA5 is involved in cell inflammation, proliferation, apoptosis, tumour cell migration, invasion, and metastasis. Moreover, SERPINA5 controls the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator secreted by the cells. SERPINA5 participtes in regulating key serine proteases which are involved in metastatic prostate disease. -
Synonyms
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
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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 MHRHHPREMK KRVEDLHVGA TVAPSSRRDF TFDLYRALAS AAPSQNIFFS PVSISMSLAM LSLGAGSSTK MQILEGLGLN LQKSSEKELH RGFQQLLQEL NQPRDGFQLS LGNALFTDLV VDLQDTFVSA MKTLYLADTF PTNFRDSAGA MKQINDYVAK QTKGKIVDLL KNLDSNAVVI MVNYIFFKAK WETSFNHKGT QEQDFYVTSE TVVRVPMMSR EDQYHYLLDR NLSCRVVGVP YQGNATALFI LPSEGKMQQV ENGLSEKTLR KWLKMFKKRQ LELYLPKFSI EGSYQLEKVL PSLGISNVFT SHADLSGISN HSNIQVSEMV HKAVVEVDES GTRAAAATGT IFTFRSARLN SQRLVFNRPF LMFIVDNNIL FLGKVNRP.
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 :
EMCN HumanDescription:
Endomucin Human Recombinant
Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.
Product # :
PRO-1156Price :
Quantity :
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Shipped with Ice Packs
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Description
EMCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (19-190 a.a) and having a molecular mass of 20.5kDa.EMCN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EMCN protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Endothelial sialomucin (Endomucin) interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix. Endomucin is expressed in the heart, kidney and lung.
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Synonyms
Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.
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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 MGSHMNSTGV LEAANNSLVV TTTKPSITTP NTESLQKNVV TPTTGTTPKG TITNELLKMS LMSTATFLTS KDEGLKATTT DVRKNDSIIS NVTVTSVTLP NAVSTLQSSK PKTETQSSIK TTEIPGSVLQ PDASPSKTGT LTSIPVTIPE NTSQSQVIGT EGGKNASTSA TSRSYSS.
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 :
ErbB2 Human, Sf9Description:
Tyrosine Kinase ErbB-2 Human Recombinant, Sf9
Receptor tyrosine-protein kinase erbB-2, EC 2.7.10.1, p185erbB2, C-erbB-2, NEU proto-oncogene, Tyrosine kinase-type cell surface receptor HER2, MLN 19, CD340 antigen, NEU, NGL, HER2, TKR1, HER-2, c-erb B2, HER-2/neu.
Product # :
PKA-094Price :
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Description
ErbB2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 638 amino acids (23-652) and having a molecular mass of 70.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ErbB2 is fused to 8 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ErbB2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HER-2/neu (erbB-2) encodes an 185-kDa orphan receptor tyrosine kinase that is constitutively active as a dimer and displays potent oncogenic activity when overexpressed. Herstatin, as the product of alternative HER-2 transcript, retains intron 8.
The herstatin mRNA is expressed in normal human fetal kidney and liver, but is at reduced levels relative to p185HER-2 mRNA in carcinoma cells that contain an amplified HER-2 gene. Herstatin appears to be an inhibitor of p185HER-2, because it disrupts dimers, reduces tyrosine phosphorylation of p185, and inhibits the anchorage-independent growth of transformed cells that overexpress HER-2. -
Synonyms
Receptor tyrosine-protein kinase erbB-2, EC 2.7.10.1, p185erbB2, C-erbB-2, NEU proto-oncogene, Tyrosine kinase-type cell surface receptor HER2, MLN 19, CD340 antigen, NEU, NGL, HER2, TKR1, HER-2, c-erb B2, HER-2/neu.
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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
TQVCTGTDMK LRLPASPETH LDMLRHLYQG CQVVQGNLEL TYLPTNASLS FLQDIQEVQG YVLIAHNQVR QVPLQRLRIV RGTQLFEDNY ALAVLDNGDP LNNTTPVTGA SPGGLRELQL RSLTEILKGG VLIQRNPQLC YQDTILWKDI FHKNNQLALT LIDTNRSRAC HPCSPMCKGS RCWGESSEDC QSLTRTVCAG GCARCKGPLP TDCCHEQCAA GCTGPKHSDC LACLHFNHSG ICELHCPALV TYNTDTFESM PNPEGRYTFG ASCVTACPYN YLSTDVGSCT LVCPLHNQEV TAEDGTQRCE KCSKPCARVC YGLGMEHLRE VRAVTSANIQ EFAGCKKIFG SLAFLPESFD GDPASNTAPL QPEQLQVFET LEEITGYLYI SAWPDSLPDL SVFQNLQVIR GRILHNGAYS LTLQGLGISW LGLRSLRELG SGLALIHHNT HLCFVHTVPW DQLFRNPHQA LLHTANRPED ECVGEGLACH QLCARGHCWG PGPTQCVNCS QFLRGQECVE ECRVLQGLPR EYVNARHCLP CHPECQPQNG SVTCFGPEAD QCVACAHYKD PPFCVARCPS GVKPDLSYMP IWKFPDEEGA CQPCPINCTH SCVDLDDKGC PAEQRASPLT LEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IMPAD1 Mouse BioactiveDescription:
Inositol Monophosphatase Domain Containing 1 Mouse Recombinant Bioactive
Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.
Product # :
PRO-2380Price :
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Description
IMPAD1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (34-356a.a.) and having a molecular mass of 36.2kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). IMPAD1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IMPAD1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 5,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze Adenosine 3, 5-diphosphate per minute at pH 7.5 at 25C.Citations
More Info
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Introduction
Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.
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Synonyms
Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.
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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
ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH HH.
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 :
FLRT3 Human, HEKDescription:
Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant, HEK
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
Product # :
PRO-2805Price :
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Description
FLRT3 Human Recombinant is a single, glycosylated, polypeptide chain (29-528 a.a) containing a total of 506 amino acids and having a molecular mass of 57.3 kDa. FLRT3 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
FLRT3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
>40%. Measured by the ability of the immobilized protein to support the adhesion of Neuro-2a neuroblast cells. When cells are added to human FLRT3 coated plates 5 ug/ml.
Citations
More Info
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Synonyms
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
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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
KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS
YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN
PTTTLNREQE KEPYKNPNLP HHHHHH. -
Background
Fibronectin leucine-rich transmembrane protein 3, commonly known as FLRT3, stands as a molecular architect in the intricate landscape of neural development. Its roles, initially discovered in the embryonic nervous system, have expanded to encompass various physiological and pathological processes in both the brain and beyond. This research endeavors to unravel the enigma of FLRT3 protein, exploring its structural intricacies, physiological functions, and its far-reaching implications in neurobiology, embryogenesis, and disease. By delving into FLRT3's multifaceted roles, scientists aim to decipher the underlying mechanisms that govern its diverse functions and explore potential therapeutic avenues in the realms of neuroscience and beyond.
Structural Complexities of FLRT3:
FLRT3 belongs to the FLRT family, characterized by extracellular leucine-rich repeats (LRRs) and a transmembrane domain. These structural motifs enable FLRT3 to participate in a myriad of interactions, including binding with cell adhesion molecules and guidance cues. Understanding the three-dimensional architecture of FLRT3 is fundamental for unraveling its molecular partnerships, biological activities, and its contributions to cell adhesion and signaling.
Physiological Functions in Neural Development:
In the developing nervous system, FLRT3 acts as a guidance molecule, steering growing axons and dendrites to their precise destinations. Through interactions with other cell surface receptors and ligands, FLRT3 modulates axon pathfinding, synapse formation, and neuronal migration. Its presence in growth cones and developing neural circuits underscores its significance in sculpting the intricate neural networks essential for proper brain function.
Beyond Neural Development:
Beyond its canonical roles in neurodevelopment, FLRT3 has emerged as a versatile player in various physiological processes. It participates in tissue morphogenesis, modulates cell adhesion, and influences immune responses. Recent studies have also implicated FLRT3 in cancer progression, highlighting its involvement in pathological conditions and making it a potential target for therapeutic interventions in cancer therapy.
FLRT3 as a Therapeutic Target:
The diverse roles of FLRT3 in neural development and diseases position it as an attractive target for therapeutic interventions. Modulating FLRT3 interactions offers novel avenues for neurological disorder treatments, including neurodevelopmental disorders and neurodegenerative diseases. Moreover, understanding FLRT3's involvement in cancer biology opens doors for innovative cancer therapies, making it a promising target for precision medicine approaches.
FLRT3, with its intricate structural features and diverse functional roles, stands as a linchpin in the realms of neuroscience, embryogenesis, and disease. Its multifaceted contributions to neural development, tissue morphogenesis, and disease pathogenesis underscore its significance in both health and pathology. As researchers continue to unravel FLRT3’s complexities, they not only deepen our understanding of fundamental biological processes but also pave the way for groundbreaking discoveries in neuroscience and therapeutic interventions, ultimately shaping the future landscape of medicine and scientific inquiry.
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 :
PLGF Human, HEKDescription:
Placental Growth Factor Human Recombinant
PIGF, PGF, PLGF-1
Product # :
CYT-1193Price :
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Description
PLGF Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-170) containing 160 amino acids and having a molecular mass of 18.3kDa.PLGF is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
PLGF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Placental Growth Factor (PLGF) which is a member of the VEGF sub-family, is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. PLGFmainly plays a role in trophoblast growth and differentiation and binds to receptor vegfr-1/flt1.
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Synonyms
PIGF, PGF, PLGF-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
DGSMAVPPQQ WALSAGNGSS EVEVVPFQEV WGRSYCRALE RLVDVVSEYP SEVEHMFSPS CVSLLRCTGC CGDENLHCVP VETANVTMQL LKIRSGDRPS YVELTFSQHV RCECRPLREK MKPERRRPKG RGKRRREKQR PTDCHLCGDA VPRRHHHHHH
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 :
AMBPDescription:
Alpha-1 Microglobulin Human Recombinant
Alpha-1-microglobulin/bikunin precursor, HCP, ITIL, ITI, EDC1, HI30, IATIL, ITILC, UTI, A1M, bikunin, complex-forming glycoprotein heterogeneous in charge, growth-inhibiting protein 19, inter-alpha-trypsin inhibitor light chain, protein AMBP, protein HC, trypstatin, uristatin, uronic-acid-rich protein.
Product # :
PRO-957Price :
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Description
AMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (20-203) and having a molecular mass of 23.1 kDa.AMBP is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AMBP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species.
A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore.
Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin.
Alpha-1-microglobulin was first discovered in pathological human urine.
It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis. -
Synonyms
Alpha-1-microglobulin/bikunin precursor, HCP, ITIL, ITI, EDC1, HI30, IATIL, ITILC, UTI, A1M, bikunin, complex-forming glycoprotein heterogeneous in charge, growth-inhibiting protein 19, inter-alpha-trypsin inhibitor light chain, protein AMBP, protein HC, trypstatin, uristatin,
uronic-acid-rich protein. -
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 MGPVPTPPDN IQVQENFNIS RIYGKWYNLA IGSTCPWLKK IMDRMTVSTL VLGEGATEAE ISMTSTRWRK GVCEETSGAY EKTDTDGKFL YHKSKWNITM ESYVVHTNYD EYAIFLTKKF SRHHGPTITA KLYGRAPQLR ETLLQDFRVV AQGVGIPEDS IFTMADRGEC VPGEQEPEPI LIPRV.
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.