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Name :
PFKM HumanDescription:
Phosphofructokinase, Muscle Human Recombinant
EC 2.7.1.11, GSD7, PFK-1, PFK1, PFKA, PFKX, Phosphofructokinase-M, Phosphofructokinase 1, Phosphohexokinase, Phosphofructo-1-kinase isozyme A, MGC8699, PFKM.
Product # :
PKA-365Price :
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Shipped with Ice Packs
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Description
PFKM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 800 amino acids (1-780 a.a.) and having a molecular mass of 87.3 kDa. PFKM protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
PFKM Human solution containing 20mM Trsi HCl pH-8, 5mM DTT, 0.2M NaCl and 20% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.
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Synonyms
EC 2.7.1.11, GSD7, PFK-1, PFK1, PFKA, PFKX, Phosphofructokinase-M, Phosphofructokinase 1, Phosphohexokinase, Phosphofructo-1-kinase isozyme A, MGC8699, PFKM.
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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). Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD GGDHIKEATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAYNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLSDLQ KAGKITDEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIMEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK AMDEKKFDEA LKLRGRSFMN NWEVYKLLAH VRPPVSKSGS HTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF QPVAELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI TRKRSGEAAV.
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 :
IL 4 MouseDescription:
Interleukin-4 Mouse Recombinant
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Product # :
CYT-282Price :
Quantity :
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Shipped at Room temp
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Description
Interleukin-4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13500 Dalton. The IL-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm concentrated (1mg/ml) solution in PBS pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.More Info
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Introduction
Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.
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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin 4 in sterile 10mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY 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 :
FGF23 HumanDescription:
Fibroblast Growth Factor-23 Human Recombinant
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Product # :
CYT-020Price :
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Shipped at Room temp
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Description
Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.
More Info
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Introduction
FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
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Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 FGF-23 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
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
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Background
Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.
Mechanism
Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.Interactions
Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.Function
Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.Structure
FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.What is the molecular weight/Mw of FGF23 HUMAN Protein?
FGF23 HUMAN Protein has a total Mw of 22.5kDa.
What is the source or expression system of FGF23 HUMAN Protein?
Escherichia Coli.
What is the Purity of FGF23 HUMAN Protein?
FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF23 HUMAN Protein?
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.
What is the amino acid sequence of FGF23 HUMAN Protein?
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
What applications can FGF23 HUMAN Protein be used in?
FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF23 HUMAN Protein?
The endotoxin level is minimal, FGF23 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IGF1 Human Des1-3Description:
Insulin-Like Growth Factor 1 Des (1-3) Human Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).
Product # :
CYT-518Price :
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Shipped at Room temp
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Description
IGF-I Des(1-3) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids (aa 4-70) and having a molecular mass of 7368.5 Dalton. IGF-1 Des1-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) was lyophilized was lyophilized from a 0.2µm filtered concentrated solution in 20mM PBS, pH 7.0.
Purity
Greater than 97.0% 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 FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5×105 units/mg.More Info
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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF-I des(1-3) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 des-1-3 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 IGF-I des(1-3) 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
TLCGAELVDA LQFVCGDRGF YFNKPTGYGS SSRRAPQTGI VDECCFRSCD LRRLEMYCAP LKPAKSA.
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 :
NECTIN1 HumanDescription:
Nectin Cell Adhesion Molecule 1 Human Recombinant
PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.
Product # :
PRO-2648Price :
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Description
NECTIN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 334amino acids (31-355a.a) and having a molecular mass of 37.3kDa.NECTIN1 is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The NECTIN1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.
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Synonyms
PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.
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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
ADPQVVQVND SMYGFIGTDV VLHCSFANPL PSVKITQVTW QKSTNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSRLELE DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL
TCKADANPPA TEYHWTTLNG SLPKGVEAQN RTLFFKGPIN YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
L-Selectin Human, Sf9Description:
L-Selectin Human Recombinant, Sf9
Selectin L, Leukocyte-Endothelial Cell Adhesion Molecule 1, CD62 Antigen-Like Family Member L, Leukocyte Surface Antigen Leu-8, Lymphocyte Adhesion Molecule 1, Lymph Node Homing Receptor, Gp90-MEL, LECAM1, LYAM1, LNHR, TQ1, Leukocyte Adhesion Molecule, Pln Homing Receptor, CD62L Antigen, L-Selectin, CD62L, PLNHR, LAM-1, LAM1, LEU8, LSEL, L-selectin.
Product # :
PRO-2487Price :
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Description
L-Selectin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 303 amino acids (52-345a.a.) and having a molecular mass of 34.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).L-Selectin is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
L-Selectin protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation. -
Synonyms
Selectin L, Leukocyte-Endothelial Cell Adhesion Molecule 1, CD62 Antigen-Like Family Member L, Leukocyte Surface Antigen Leu-8, Lymphocyte Adhesion Molecule 1, Lymph Node Homing Receptor, Gp90-MEL, LECAM1, LYAM1, LNHR, TQ1, Leukocyte Adhesion Molecule, Pln Homing Receptor, CD62L Antigen, L-Selectin, CD62L, PLNHR, LAM-1, LAM1, LEU8, LSEL, L-selectin.
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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
ADPWTYHYSE KPMNWQRARR FCRDNYTDLV AIQNKAEIEY LEKTLPFSRS YYWIGIRKIG GIWTWVGTNK SLTEEAENWG DGEPNNKKNK EDCVEIYIKR NKDAGKWNDD ACHKLKAALC YTASCQPWSC SGHGECVEII NNYTCNCDVG YYGPQCQFVI QCEPLEAPEL GTMDCTHPLG NFSFSSQCAF SCSEGTNLTG IEETTCGPFG NWSSPEPTCQ VIQCEPLSAP DLGIMNCSHP LASFSFTSAC TFICSEGTEL IGKKKTICES SGIWSNPSPI CQKLDKSFSM IKEGDYNHHH HHH.
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 :
GATM HumanDescription:
Glycine Amidinotransferase Human Recombinant
Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.
Product # :
ENZ-583Price :
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Description
GATM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (38-423) and having a molecular mass of 46.9kDa (Molecular size on SDS-PAGE will appear higher).GATM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GATM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Glycine amidinotransferase mitochondrial (GATM) is a mitochondrial enzyme which is a member of the amidinotransferase family. The GATM enzyme is involved in creatine biosynthesis, where it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine, which has an imperative role in energy metabolism in muscle tissues. GATM is significant in embryonic and central nervous system development. GATM gene mutations cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.
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Synonyms
Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.
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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 MGSMSTQAAT ASSRNSCAAD DKATEPLPKD CPVSSYNEWD PLEEVIVGRA ENACVPPFTI EVKANTYEKY WPFYQKQGGH YFPKDHLKKA VAEIEEMCNI LKTEGVTVRR PDPIDWSLKY KTPDFESTGL YSAMPRDILI VVGNEIIEAP MAWRSRFFEY
RAYRSIIKDY FHRGAKWTTA PKPTMADELY NQDYPIHSVE DRHKLAAQGK FVTTEFEPCF DAADFIRAGR DIFAQRSQVT NYLGIEWMRR HLAPDYRVHI ISFKDPNPMH IDATFNIIGP GIVLSNPDRP CHQIDLFKKA GWTIITPPTP IIPDDHPLWM SSKWLSMNVL MLDEKRVMVD
ANEVPIQKMF EKLGITTIKV NIRNANSLGG GFHCWTCDVR RRGTLQSYLD.
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 :
CD116 HumanDescription:
GM-CSF Receptor Alpha Human Recombinant
CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.
Product # :
CYT-796Price :
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- sds-page
Description
CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (20-320 a.a) and having a molecular mass of 37.2kDa.CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSF2RA 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.
sds-page
More Info
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Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
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Synonyms
CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.
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Physical Appearance
Sterile Filtered clear 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.
-
Background
Unlocking the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Implications and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) plays a pivotal role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper examines the significance of Human Recombinant CNTFR, its production techniques, and its potential applications in neurobiology and therapeutic interventions. The review underscores CNTFR's crucial role in advancing neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, is central to transducing the signals initiated by CNTF. Availability of Human Recombinant CNTFR enables researchers to dissect its contribution to neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's role in modulating neuronal health and promoting regeneration makes it a cornerstone in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and trigger downstream signaling pathways. Activation of intracellular cascades, such as JAK/STAT and MAPK, is instrumental in driving the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is generated through gene expression in suitable host cells, often utilizing bacterial or mammalian systems. Ensuring accurate folding and post-translational modifications is crucial to preserve its functionality and affinity for CNTF.
Therapeutic Applications:
Human Recombinant CNTFR holds promise for therapeutic applications in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-associated signaling presents opportunities to bolster neuronal survival and regeneration, potentially revolutionizing patient care.
Challenges and Future Directions:
While the potential is significant, challenges encompass optimizing CNTFR-CNTF interactions, effective tissue delivery, and understanding potential off-target effects. Ongoing research is paramount to unravel the complete mechanisms of CNTFR-mediated signaling and its therapeutic implications.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor emerges as a vital tool in advancing our grasp of neuroprotection and regeneration. Its capacity to modulate CNTF effects opens doors to innovative therapeutic strategies for addressing neurodegenerative disorders, embodying the intersection of molecular insights and clinical progress.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 37.2kDa.
What is the source or expression system of CD116 Protein?
Escherichia Coli.
What is the Purity of CD116 Protein?
CD116 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CD116 Protein?
The biological functionality of CD116 Protein will be determined in the future.
What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 324 amino acids.
What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 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 :
ACOT13 HumanDescription:
Acyl-CoA Thioesterase 13 Human Recombinant
Acyl-coenzyme A thioesterase 13, Acyl-CoA thioesterase 13, Thioesterase superfamily member 2, ACOT13, THEM2, HT012, MGC4961, PNAS-27, ACOT13.
Product # :
ENZ-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACOT13 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.1kDa. The ACOT13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACOT13 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Acyl-coenzyme A thioesterase 13 (ACOT13) belongs to the thioesterase subfamily of esterase family. ACOT13 is highly expressed in the kidney with moderate expression in the brain, liver and intestines. ACOT13 contains a hotdog-fold and is thought to co-localize with microtubules, possibly having a role in cellular proliferation events. Deletion of a segment of the q arm of chromosome 6 is linked to early onset intestinal cancer, suggesting the presence of a cancer susceptibility locus.
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Synonyms
Acyl-coenzyme A thioesterase 13, Acyl-CoA thioesterase 13, Thioesterase superfamily member 2, ACOT13, THEM2, HT012, MGC4961, PNAS-27, ACOT13.
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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 MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN.
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 :
S100A3 MouseDescription:
S100 Calcium Binding Protein A3 Mouse Recombinant
Protein S100-A3, Protein S-100E, S100 calcium-binding protein A3, S100a3, S100E.
Product # :
PRO-1166Price :
Quantity :
Shipping Method :
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Description
S100A3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-101 a.a) and having a molecular mass of 14.3kDa.S100A3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 2mM DTT and 150mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.
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Synonyms
Protein S100-A3, Protein S-100E, S100 calcium-binding protein A3, S100a3, S100E.
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Physical Appearance
S100A3 is supplied as a sterile filtered clear 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 MGSHMTRPLE QAVAAIVCTF QEYAGRCGDK YKICQSELKE LLQKELPTWT PSEFRECDYN KFMSVLDTNK DCEVDFGEYV RSLASLCLYC HEYFKECPPE PPCPQ.
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 :
S100G HumanDescription:
S100 Calcium Binding Protein G Human Recombinant
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
Product # :
PRO-156Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human S100G produced in E.coli has a molecular mass of 10.04kDa containing 87 amino acid residues of the human S100G and fused to a 9 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
S100G was filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
More Info
-
Introduction
S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.
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Synonyms
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS TKKSPEELKRS TKKSPEELKR IFEKYAAKEG DPDQLSKDEL KLLIQAEFPS LLKGPNTLDD LFQELDKNGD GEVSFEEFQV LVKKISQ.
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Applications
Western blotting.
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 :
DCUN1D4 HumanDescription:
DCN1 Defective in Cullin Neddylation 1 Domain Containing 4 Human Recombinant
DCN1 Defective In Cullin Neddylation 1 Domain Containing 4, Defective In Cullin Neddylation Protein 1-Like Protein 4, DCUN1 Domain-Containing Protein 4, KIAA0276, DCN1-Like Protein 4.
Product # :
PRO-1715Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCUN1D4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 36.5kDa.DCUN1D4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DCUN1D4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
DCUN1D4 holds 1 DCUN1 domain.
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Synonyms
DCN1 Defective In Cullin Neddylation 1 Domain Containing 4, Defective In Cullin Neddylation Protein 1-Like Protein 4, DCUN1 Domain-Containing Protein 4, KIAA0276, DCN1-Like Protein 4.
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Physical Appearance
Sterile Filtered clear 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 MGSMHSDAAA VNFQLNSHLS TLANIHKIYH TLNKLNLTED IGQDDHQTGS LRSCSSSDCF NKVMPPRKKR RPASGDDLSA KKSRHDSMYR KYDSTRIKTE EEAFSSKRCL EWFYEYAGTD DVVGPEGMEK FCEDIGVEPE NVVMLVLAWK LDAQNMGYFT LQEWLKGMTS LQCDTTEKLR NTLDYLRSFL NDSTNFKLIY RYAFDFAREK DQRSLDINTA KCMLGLLLGK IWPLFPVFHQ FLEQSKYKVI NKDQWCNVLE FSRTINLDLS NYDEDGAWPV LLDEFVEWYK DKQMS
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 :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
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Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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Physical Appearance
Sterile Filtered clear 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 MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
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 :
NFKBID HumanDescription:
NF-kappa-B Inhibitor Delta Human Recombinant
NF-kappa-B inhibitor delta, I-kappa-B-delta, IkB-delta, IkappaBdelta, IkappaBNS, T-cell activation NFKB-like protein, TA-NFKBH, NFKBID, IKBNS.
Product # :
PRO-1684Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NFKBID Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313) and having a molecular mass of 35.9 kDa.NFKBID is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NFKBID solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
NFKBID belongs to the IkB family of proteins which contains four groups (IkB-alpha, IkB-beta, IkB-gamma, IkB-epsilon). NFKBID takes part in regulating inflammatory responses and cytokine, IL-2 and IL-6 expression through NFkB activity. NFKBID has 3 known alternative spliced isoforms, and is associated with RelB, NF?B p50 and NFkB p65 in nucleus. NFKBID is involeved in thymocyte selection in response to TCR induction.
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Synonyms
NF-kappa-B inhibitor delta, I-kappa-B-delta, IkB-delta, IkappaBdelta, IkappaBNS, T-cell activation NFKB-like protein, TA-NFKBH, NFKBID, IKBNS.
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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 MGSMEAGPWR VSAPPSGPPQ FPAVVPGPSL EVARAHMLAL GPQQLLAQDE EGDTLLHLFA ARGLRWAAYA AAEVLQVYRR LDIREHKGKT PLLVAAAANQ PLIVEDLLNL GAEPNAADHQ GRSVLHVAAT YGLPGVLLAV LNSGVQVDLE ARDFEGLTPL HTAILALNVA MRPSDLCPRV LSTQARDRLD CVHMLLQMGA NHTSQEIKSN KTVLHLAVQA ANPTLVQLLL ELPRGDLRTF VNMKAHGNTA LHMAAALPPG PAQEAIVRHL LAAGADPTLR NLENEQPVHL LRPGPGPEGL RQLLKRSRVA PPGLSS.
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 :
ASS1 HumanDescription:
Argininosuccinate Synthase 1 Human Recombinant
ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.
Product # :
ENZ-548Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 432 amino acids (1-412 a.a.) and having a molecular mass of 48.6 kDa. The ASS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ASS1 Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.
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Synonyms
ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK.
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 :
Bax Mouse, GSTDescription:
Bax Mouse Recombinant, GST
Apoptosis regulator BAX membrane isoform alpha, Bax, Bcl2-associated X protein.
Product # :
PRO-647Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
- purity
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Description
Bax Mouse Recombinant amino acid 1-171 produced in E.Coli is a single, non-glycosylated polypeptide chain. The Mouse Bax is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The 1mg/ml protein contains 10mM Tris-HCl pH-8, 1mM EDTA and 150mM NaCl, 10% glycerol, 0.1% tween & 10mM glutathione.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Bcl-2–associated X protein (Bax) belongs to the Bcl-2 protein family.
Bax is a pro-apoptotic Bcl-2 protein containing BH1, BH2 and BH3 domains.
Bax accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor bcl2 or its adenovirus homolog e1b 19k protein. Bax induces the release of cytochrome c, activation of casp3, and thereby apoptosis. Bax is expressed in a wide variety of tissues, with highest levels in the testis and ovary.
Tumor suppressor protein p53 upregulates the expression of BAX. Bax has been shown to be involved in p53-mediated apoptosis. -
Synonyms
Apoptosis regulator BAX membrane isoform alpha, Bax, Bcl2-associated X protein.
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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.
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 :
IL 20 MouseDescription:
Interleukin-20 Mouse Recombinant
IL10D, ZCYTO10, IL-20, MGC96907, Four alpha helix cytokine Zcyto10.
Product # :
CYT-379Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-20 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a total molecular mass of 17,584 Dalton. The IL-20 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by measuring the dose dependent activation of STAT3 in human epidermal keratinocytes (HEK2a cells). Significant STAT3 activation is observed with >100ng/mL of Interleukin-20 recombinant mouse, corresponding to a specific activity of 10,000 units/mg of Interleukin-20 recombinant mouse.More Info
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Introduction
IL20 is a cytokine structurally related to interleukin 10 (IL10). IL20 cytokine has been shown to transduce its signal through signal transducer and activator of transcription 3 (STAT3) in keratinocytes. A specific receptor for this cytokine is found to be expressed in skin and upregulated dramatically in psoriatic skin, suggesting a role for this protein in epidermal function and psoriasis.
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Synonyms
IL10D, ZCYTO10, IL-20, MGC96907, Four alpha helix cytokine Zcyto10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL20 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-20 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
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Lys-Thr-Leu.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.552 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-20 as a Reference Standard.
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 :
EXOSC4 HumanDescription:
Exosome Component 4 Human Recombinant
Exosome Component 4, Ribosomal RNA-Processing Protein 41, Exosome Complex Exonuclease RRP41, Exosome Complex Component RRP41, RRP41A, Ski6p, SKI6, p12A.
Product # :
PRO-1792Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EXOSC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 268 amino acids (1-245aa) and having a molecular mass of 28.8kDa.EXOSC4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EXOSC4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
EXOSC4 is a Non-catalytic component of the RNA exosome complex that has 3'->5' exoribonuclease activity and takes part in several cellular RNA processing and degradation procedures. In the nucleus, the RNA exosome complex contributes to accurate maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the removal of RNA processing by-products and non-coding 'pervasive' transcripts, like antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing deficiencies, thus controlling or excluding their export to the cytoplasm. Diseases related with EXOSC4 include hepatitis a, and mouth disease.
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Synonyms
Exosome Component 4, Ribosomal RNA-Processing Protein 41, Exosome Complex Exonuclease RRP41, Exosome Complex Component RRP41, RRP41A, Ski6p, SKI6, p12A.
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Physical Appearance
Sterile Filtered clear 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 MGSMAGLELL SDQGYRVDGR RAGELRKIQA RMGVFAQADG SAYIEQGNTK ALAVVYGPHE IRGSRARALP DRALVNCQYS SATFSTGERK RRPHGDRKSC EMGLQLRQTF EAAILTQLHP RSQIDIYVQV LQADGGTYAA CVNAATLAVL DAGIPMRDFV CACSAGFVDG TALADLSHVE EAAGGPQLAL ALLPASGQIA LLEMDARLHE DHLERVLEAA AQAARDVHTL LDRVVRQHVR EASILLGD
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 :
CXCL14 MouseDescription:
BRAK (CXCL14) Mouse Recombinant
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
Product # :
CHM-007Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
CXCL14 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 500mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 of CXCL14 as determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 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
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
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Background
What is the molecular weight/Mw of CXCL14 MOUSE Protein?
CXCL14 MOUSE Protein has a total Mw of 9.4kDa.
What is the source or expression system of CXCL14 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL14 MOUSE Protein?
CXCL14 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 MOUSE Protein?
The ED50 of CXCL14 as determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.
What is the amino acid sequence of CXCL14 MOUSE Protein?
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
What applications can CXCL14 MOUSE Protein be used in?
CXCL14 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 MOUSE Protein?
The endotoxin level is minimal, CXCL14 MOUSE 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 :
PFN1 RatDescription:
Profilin-1 Rat Recombinant
Profilin-1, Profilin I.
Product # :
PRO-2231Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- purity
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Description
PFN1 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 17.5kDa. PFN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PFN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Profilin-1 also known as Pfn1 is a ubiquitous actin monomer-binding protein which is a member of the profilin family. Pfn1 significantly enhances skin wound healing in-vitro as well as in-vivo which is mediated by purinergic receptors. Furthermore, Pfn1 is also active in endothelial cell migration and vessel sprouting. Pfn1 is considered to regulate actin polymerization in response to extracellular signals.
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Synonyms
Profilin-1, Profilin I.
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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 MGSHMAGWNA YIDSLMADGT CQDAAIVGYK DSPSVWAAVP GKTFVSITPA EVGVLVGKDR SSFFVNGLTL GGQKCSVIRD SLLQDGEFTM DLRTKSTGGA PTFNVTVTMT AKTLVLLMGK EGVHGGLINK KCYEMASHLR RSQY.
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 :
FGFR1OP HumanDescription:
FGFR1 Oncogene Partner Human Recombinant
FGFR1 oncogene partner, FGFR1OP, FOP.
Product # :
PKA-031Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FGFR1OP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-379 a.a) and having a molecular mass of 43.5kDa.FGFR1OP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FGFR1OP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
FGFR1 oncogene partner (FGFR1OP) is a member of the FGFR1OP family. The FGFR1OP protein is an essentially hydrophilic protein proposed to be a leucine-rich protein family member. A t(6;8)(q27;p11) chromosomal translocation, fusing the FGFR1OP gene and the FGFR1 gene, is seen in cases of myeloproliferative disorder. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP gene is believed to play a significant role in normal proliferation and differentiation of the erythroid lineage.
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Synonyms
FGFR1 oncogene partner, FGFR1OP, FOP.
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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 MGSHMAATAA AVVAEEDTEL RDLLVQTLEN SGVLNRIKAE LRAAVFLALE EQEKVENKTP LVNESLKKFL NTKDGRLVAS LVAEFLQFFN LDFTLAVFQP ETSTLQGLEG RENLARDLGI IEAEGTVGGP LLLEVIRRCQ QKEKGPTTGE GALDLSDVHS PPKSPEGKTS AQTTPSKKAN DEANQSDTSV SLSEPKSKSS LHLLSHETKI GSFLSNRTLD GKDKAGLCPD EDDMEGDSFF DDPIPKPEKT YGLRKEPRKQ AGSLASLSDA PPLKSGLSSL AGAPSLKDSE SKRGNTVLKD LKLISDKIGS LGLGTGEDDD YVDDFNSTSH RSEKSEISIG EEIEEDLSVE IDDINTSDKL DDLTQDLTVS QLSDVADYLE DVA.
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 :
TIMP1 Human, Sf9Description:
Tissue Inhibitor of Metalloprotease 1 Human Recombinant, Sf9
TIMP Metallopeptidase Inhibitor 1, TIMP, EPA, Tissue Inhibitor Of Metalloproteinases 1, Fibroblast Collagenase Inhibitor, Erythroid-Potentiating Activity, Collagenase Inhibitor, TIMP-1, CLGI, Tissue Inhibitor Of Metalloproteinase 1 (Erythroid Potentiating Activity, Collagenase Inhibitor), Erythroid Potentiating Activity, Metalloproteinase Inhibitor 1, EPO, HCI, Metalloproteinase inhibitor 1.
Product # :
ENZ-876Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TIMP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (24-207a.a.) and having a molecular mass of 21.5kDa. TIMP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TIMP1 protein solution (0.2mg/ml) contains phosphate buffered saline (pH7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells. The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds. TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones.
Increased TIMP1 levels are connected with squamous cell laryngeal carcinoma. TIMP1 overexpression is linked to gastric cancer. -
Synonyms
TIMP Metallopeptidase Inhibitor 1, TIMP, EPA, Tissue Inhibitor Of Metalloproteinases 1, Fibroblast Collagenase Inhibitor, Erythroid-Potentiating Activity, Collagenase Inhibitor, TIMP-1, CLGI, Tissue Inhibitor Of Metalloproteinase 1 (Erythroid Potentiating Activity, Collagenase Inhibitor), Erythroid Potentiating Activity, Metalloproteinase Inhibitor 1, EPO, HCI, Metalloproteinase inhibitor 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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 :
PIP ProteinDescription:
Prolactin-Induced Protein Human Recombinant
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
Product # :
CYT-793Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
PIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (29-146 a.a.) and having a molecular mass of 15.9kDa.PIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PIP protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Prolactin-inducible protein (PIP) is a main protein component of benign breast gross cysts. PIP is a famous indicator of breast cancer, since it is found in around 50% of all breast cancer specimens. PIP is expressed in exocrine glands, in pathologic conditions, in breast cysts and breast cancers exhibiting apocrine features. PIP and prostate specific antigen are co-expressed in androgen receptor-positive breast tumours.
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Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
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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 MGSQDNTRKI IIKNFDIPKS VRPNDEVTAV LAVQTELKEC MVVKTYLISS IPLQGAFNYK YTACLCDDNP KTFYWDFYTN RTVQIAAVVD VIRELGICPD DAAVIPIKNN RFYTIEILKV E.
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 :
FSCN1 HumanDescription:
Recombinant Human Fascin
Strongylocentrotus Purpuratus, actin-bundling protein, FAN1, HSN, SNL.
Product # :
PRO-527Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- purity
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Description
FSCN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 513 amino acids (1-493 a.a.) and having a molecular mass of 56.7 kDa. The FSCN1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
FSCN1 is an actin-bundling protein that is responsible for rigidity to filopodial bundles to efficiently push the membrane forward during cytoskeleton remodeling and cell migration. FSCN1 takes part in the gathering of actin filament bundles present in microspikes, membrane ruffles, and stress fibers. FSCN1 is absent from most normal epithelia though is upregulated in multiple forms of human carcinoma, where its expression associates clinically with a poor prognosis. FSCN1 expression is abundantly found in neurons, glial cells, and endothelial cells.
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Synonyms
Strongylocentrotus Purpuratus, actin-bundling protein, FAN1, HSN, SNL.
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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 MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV CLRSHLGRYL
AADKDGNVTC EREVPGPDCR FLIVAHDDGR WSLQSEAHRR YFGGTEDRLS CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA
DEIAVDRDVP WGVDSLITLA FQDQRYSVQT ADHRFLRHDG RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL KAGKATKVGK
DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW
RDRRITLRAS NGKFVTSKKN GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND GAYNIKDSTG
KYWTVGSDSA VTSSGDTPVD FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA SAETVDPASL WEY.
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.