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1000 results found for “haptoglobin”
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Name :
TAF15 HumanDescription:
TAF15 Human Recombinant
Npl3, RBP56, TAF2N, TAFII68, TATA-binding protein-associated factor 2N, 68 kDa TATA-binding protein-associated factor, RNA-binding protein 56, TAF15.
Product # :
PRO-1805Price :
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Description
TAF15 Human Recombinant produced in E. coli is. a single polypeptide chain containing 282 amino acids (148-406) and having a molecular mass of 30kDa. TAF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TAF15 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TAF15 is a member of the TET family of RNA-binding proteins. TAF15 is a component of a subset of multi-subunit transcription initiation factor TFIID complexes which takes part in RNA polymerase II gene transcription. Translocations involving TAF15 are found in severe leukemia and extraskeletal myxoid chondrosarcoma. Mutations in TAF15 take part in amyotrophic lateral sclerosis.
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Synonyms
Npl3, RBP56, TAF2N, TAFII68, TATA-binding protein-associated factor 2N, 68 kDa TATA-binding protein-associated factor, RNA-binding protein 56, TAF15.
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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 MGSSYHSQRE NYSHHTQDDR RDVSRYGEDN RGYGGSQGGG RGRGGYDKDG RGPMTGSSGG DRGGFKNFGG HRDYGPRTDA DSESDNSDNN TIFVQGLGEG VSTDQVGEFF KQIGIIKTNK KTGKPMINLY TDKDTGKPKG EATVSFDDPP SAKAAIDWFD GKEFHGNIIK VSFATRRPEF MRGGGSGGGR RGRGGYRGRG GFQGRGGDPK SGDWVCPNPS CGNMNFARRN SCNQCNEPRP EDSRPSGGDF RGRGYGGERG YR.
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 :
GSTP1 HumanDescription:
Glutathione S-Transferase pi 1 Human Recombinant
Glutathione S-transferase P, GST class-pi, GSTP1-1, GSTP1, FAEES3, GST3, PI, DFN7.
Product # :
ENZ-427Price :
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Description
GSTP1 Human Recombinant fused with 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (1-210 a.a.) And having a molecular mass of 27.4kDa. The GSTP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH7.0), 30% glycerol, 1mM EDTA and 0.1mM PMSF.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 80 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.
Citations
More Info
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Introduction
GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells. -
Synonyms
Glutathione S-transferase P, GST class-pi, GSTP1-1, GSTP1, FAEES3, GST3, PI, DFN7.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPPY TVVYFPVRGR CAALRMLLAD QGQSWKEEVV TVETWQEGSL KASCLYGQLP KFQDGDLTLY QSNTILRHLG RTLGLYGKDQ QEAALVDMVN DGVEDLRCKY ISLIYTNYEA GKDDYVKALP GQLKPFETLL SQNQGGKTFI VGDQISFADY NLLDLLLIHE VLAPGCLDAF PLLSAYVGRL SARPKLKAFL ASPEYVNLPI NGNGKQ.
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 :
HMOX1 HumanDescription:
Heme Oxygenase 1 Human Recombinant
HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.
Product # :
ENZ-392Price :
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Description
HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids (1-266) and having a molecular mass of 31.4 kDa. HO-1 is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMOX1 1 mg/ml solution containing 20mM Tris-HCl pH-8, 50mM NaCl, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function and its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, and TNF-alpha in murine and human macrophages.
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Synonyms
HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.
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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
MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH.
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 :
AZGP1 Human, HEKDescription:
Alpha-2-Glycoprotein 1 Zinc-Binding Human Recombinant, HEK
Zn-alpha-2-glycoprotein, Zn-alpha-2-GP, AZGP1, ZAG, Zinc-alpha-2-glycoprotein, ZNGP1, ZA2G.
Product # :
PRO-403Price :
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Description
ZA2G Human Recombinant produced in HEK cells is a single, glycosylated polypeptide chain containing a total of 290 amino acids encoding (13-290). ZA2G Human Recombinant is identical to Swiss-Prot-P25311 (AA 18-295, mature Zinc-Alpha-2-Glycoprotein). Twelve extra amino acids were fused with the N-terminus.
Source
293 Cell Line (Human Embryonic Kidney).
Formulation
Filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 0.1M Tris-HCl pH 8.0 and 150mM NaCl.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Differentiated human SGBS adipocytes were incubated for 18 h at two dose levels of rhZA2G - 5 and 20 µg/ml. Lipolysis was quantified by measuring glycerol release into the medium using a standard protocol. Isoproterenol (10 µM) and IBMX (100 µM) were used as positive controls. "Con" stands for the negative control. There was a 3-fold increase in glycerol release with both doses. The increase was statistically significant at 5 µg/ml dose of rhZA2G (p<0.01) as well as in positive controls.Citations
More Info
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Introduction
Zinc-alpha-2-glycoprotein (ZAG) is found in body fluids such as serum, sweat, and seminal and breast cyst fluids. It is identical in amino acid sequence to tumor-derived lipid mobilizing factor (LMF), a protein associated with the dramatic loss of adipose body stores in cancer cachexia, and has been shown to stimulate lipolysis by adipocytes in vivo and in vitro. A role for ZAG has been proposed in the regulation of body weight, and age-dependent changes in genetically influenced obesity, and also it regulates melanin production by normal and malignant melanocytes. It has also recently been classified as a novel adipokine in that it is produced by both white and brown fat adipocytes and may act in a local autocrine fashion in the reduction of adiposity in cachexia. Controlling ZAG/LMF's activity could be life-saving in the management of certain cancers and other cachexiainducing conditions, and its possible normal role in body fat store homeostasis is deserving of understanding in its own right. ZAG exhibits a class I major histocompatibility complex (MHC) fold but is a soluble protein rather than being anchored to plasma membranes and does not associate with alpha-2-microglobulin in humans. Like antigen-presenting MHC class I proteins, ZAG has an open apical groove, and X-ray crystallography of human derived ZAG revealed an unidentifiable electron density in a similar position to that occupied by antigenic peptides in classical MHC proteins and glycolipids in isoforms of CD1. This presumptive ligand is not a peptide, and the groove is too small to hold a glycolipid such as is presented by CD1 isoforms. By analogy with all other MHC class I-related proteins that have an open apical groove [some do not ], occupancy by a ligand is probably crucial to ZAG's biological function. Despite all of the structural and biochemical evidence that ZAG binds a ligand, none has so far been found by extraction from protein isolated from biological fluids. This difficulty could be because the ligand is labile, heterogeneous, or readily lost during purification procedures. Knowing more about how ZAG interacts with the compounds it has been found to bind, both natural and artificial, will inform searches for the elusive ligand(s) and its/their role in ZAG's signaling function.
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Synonyms
Zn-alpha-2-glycoprotein, Zn-alpha-2-GP, AZGP1, ZAG, Zinc-alpha-2-glycoprotein, ZNGP1, ZA2G.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ZA2G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ZA2G 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 avoid freeze-thaw cycles.
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Solubility
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
ASWSHPQFEK GSQENQDGRY SLTYIYTGLS KHVEDVPAFQ ALGSLNDLQF FRYNSKDRKS QPMGLWRQVEGMEDWKQDSQ LQKAREDIFM ETLKDIVEYY NDSNGSHVLQ GRFGCEIENN RSSGAFWKYY YDGKDYIEFNKEIPAWVPFD PAAQITKQKW EAEPVYVQRA KAYLEEECPA TLRKYLKYSK NILDRQDPPS VVVTSHQAPG EKKKLKCLAYDFYPGKIDVH WTRAGEVQEP ELRGDVLHNG NGTYQSWVVV AVPPQDTAPY SCHVQHSSLA QPLVVPWEAS.
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 :
Avidin RecombinantDescription:
Avidin Recombinant
Avidin, AVD, AVID.
Product # :
PRO-2597Price :
Quantity :
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Shipped at Room temp
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Description
Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.
Source
Corn (Zea Mays).
Purity
Greater than 90% as visualized by SDS-PAGE.
Biological Activity
13.5 units/mg protein, 1 unit binds 1µg biotin.
Citations
More Info
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Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
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Synonyms
Avidin, AVD, AVID.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Recombinant Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant Avidin 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 Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Borrelia OspCDescription:
Borrelia Burgdorferi Outer Surface Protein C Recombinant
Product # :
BOR-004Price :
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Description
Recombinant Borrelia Burgdorferi Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 26kDa. Borrelia OspC is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia OspC is supplied in 16mM HEPES buffer pH-7.0, 300mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Applications
Western blot with Lyme positive plasma.
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 :
KLRC2 HumanDescription:
Killer Cell Lectin-Like Receptor Subfamily C, Member 2 Human Recombinant
Killer cell lectin-like receptor subfamily C member 2, NKG2-C type II integral membrane protein, NKG2-C-activating NK receptor, CD159 antigen-like family member C, NK cell receptor C, NKG2C, CD159c.
Product # :
PRO-1190Price :
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Description
KLRC2 Human Recombinant produced in E. coli is a single polypeptide chain containing 162 amino acids (94-231) and having a molecular mass of 18.4 kDa.KLRC2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The KLRC2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
KLRC2 has a part as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. The group, designated KLRC (NKG2) are expressed mainly in natural killer (NK) cells and encodes a family of transmembrane proteins categorized by a type II membrane orientation (extracellular C terminus) and the presence of a C-type lectin domain. The KLRC (NKG2) gene family is situated inside the NK complex, a region which holds a few C-type lectin genes specially expressed on NK cells. KLRC2 alternative splice variants are known but their full-length nature is yet to be determined.
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Synonyms
Killer cell lectin-like receptor subfamily C member 2, NKG2-C type II integral membrane protein, NKG2-C-activating NK receptor, CD159 antigen-like family member C, NK cell receptor C, NKG2C, CD159c.
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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 NNFSPNTRTQ KARHCGHCPE EWITYSNSCY YIGKERRTWE ESLLACTSKN SSLLSIDNEE EMKFLASILP SSWIGVFRNS SHHPWVTING LAFKHKIKDS DNAELNCAVL QVNRLKSAQC GSSMIYHCKH KL
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 :
BNP HumanDescription:
B-type Natriuretic Peptide Human
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-369Price :
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Shipped at Room temp
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Description
B-type Natriuretic Peptide Human is a polypeptide chain containing 32 amino acids and having a molecular mass of 3464 Dalton. The molecular formula is:C143H244N50O42S4.
Formulation
The protein was lyophilized without additives.
Purity
Greater than 95.0% as determined by RP-HPLC.
Citations
More Info
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Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized B-type Natriuretic Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution B-type Natriuretic Peptide should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized B-type Natriuretic Peptide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
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Background
What is the molecular weight / Mw of BNP Human?
BNP Human has a total Mw of 3.4kDa.
What is the source or expression system of BNP Human?
Synthetic.
What is the Purity of BNP Human?
BNP Human is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BNP Human?
The biological functionality of BNP Human will be determined in the future.
What is the amino acid sequence of BNP Human?
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
What applications can BNP Human Protein be used in?
BNP Human can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BNP Human?
The endotoxin level is minimal, BNP Human 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 :
TNNI3 Human NativeDescription:
Cardiac Troponin-I Human
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Product # :
PRO-2788Price :
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Description
TNNI3 Native produced in Human heart tissue is a full length protein which has an additional amino acid residues on its N terminus that are not present on the skeletal form, making this protein a promising analyte for indicating cardiac specificity.TNNI3 Native is purified by proprietary chromatographic technique.
Source
Human heart tissue.
Formulation
TNNI3 was lyophilized from 0.01M HCl.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiac Troponin-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 TNNI3 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Troponin I, encoded by the TNNI3 gene, is a critical component of the troponin complex in cardiac muscle cells. It plays a central role in the regulation of cardiac muscle contraction by modulating the interaction between actin and myosin filaments.
While extensive research has been conducted on troponin I in the context of cardiac diseases, there is a growing need to investigate native human troponin I (TNNI3) in its unmodified form to gain a deeper understanding of its functions, structural significance, and implications for heart health. This research aims to provide a comprehensive exploration of TNNI3 in its native state, shedding light on its various roles and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the physiological role of native human TNNI3 in cardiac muscle contraction. Experiments involving human cardiac tissue samples and isolated myocytes will be conducted to investigate how TNNI3 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of cardiac muscle physiology and its implications for heart health.
The second objective is to assess the clinical relevance of native TNNI3 in cardiac diseases. Clinical studies involving patients with various cardiac conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI3 as a biomarker. These investigations may provide valuable insights into the use of native TNNI3 in the early detection and management of heart diseases.
The third objective is to explore the potential applications of native TNNI3 in biomedical research and drug development. Research will investigate the use of native TNNI3-expressing cells as models for studying cardiac disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human TNNI3, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology and biomedical research.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HSV-2 VP22Description:
Herpes Simplex Virus-2 VP22 Recombinant
Product # :
HSV-228Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived Full length HSV-2 VP22 recombinant protein is fused to a Six histidine tag at C-terminus and has a MW of 33,5kDa (pI 10.5).
Source
Escherichia Coli.
Formulation
10 mM Phosphate buffer pH 7.6; 75 mM NaCl.
Purity
Protein is >90% pure as determined by SDS PAGE.
Citations
More Info
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Introduction
Entry of HSV into the host cell involves interactions of several viral glycoproteins with cell surface receptors. The virus particle is covered by an envelope which, when bound to specific receptors on the cell surface, will fuse with the cell membrane and create an opening, or pore, through which the virus enters the host cell. The sequential stages of HSV entry are analagous to those of other viruses. At first, complementary receptors on the virus and cell surface bring the two membranes into proximity. In an intermediate state, the two membranes begin to merge, forming a hemifusion state. Finally, a stable entry pore is formed through which the viral envelope contents are introduced to the host cell.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
HSV-2 VP22 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
ELISA, WB, Flow-Through.
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 :
MIP 1a HumanDescription:
Macrophage Inflammatory Protein-1 Alpha Human Recombinant (CCL3)
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.
Product # :
CHM-233Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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Description
Macrophage Inflammatory Protein-1 alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 0.55 mg/ml solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.Citations
More Info
-
Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophilsand basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 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 Macrophage Inflammatory Protein-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Ser-Leu-Ala-Ala.
-
Background
What is the molecular weight/Mw of MIP 1A HUMAN Protein?
MIP 1A HUMAN Protein has a total Mw of 7.82kDa.
What is the source or expression system of MIP 1A HUMAN Protein?
Escherichia Coli.
What is the Purity of MIP 1A HUMAN Protein?
MIP 1A HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A HUMAN Protein?
The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of MIP 1A HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Ser-Leu-Ala-Ala.
What applications can MIP 1A HUMAN Protein be used in?
MIP 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A HUMAN Protein?
The endotoxin level is minimal, MIP 1A HUMAN Protein was purified using conventional chromatography techniques.Who supplies recombinant MIP 1A 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 MIP 1A 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 :
MIP 1a MouseDescription:
Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3)
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.
Product # :
CHM-320Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
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Description
Macrophage Inflammatory Protein-1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 1mg/ml solution containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.Citations
More Info
-
Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 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.
-
Solubility
It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.
-
Background
What is the molecular weight/Mw of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein has a total Mw of 7.82kDa.
What is the source or expression system of MIP 1A MOUSE Protein?
Escherichia Coli.
What is the Purity of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A MOUSE Protein?
The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of MIP 1A MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.
What applications can MIP 1A MOUSE Protein be used in?
MIP 1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A MOUSE Protein?
The endotoxin level is minimal, MIP 1A MOUSE Protein was purified using conventional chromatography techniques.Who supplies recombinant MIP 1A MOUSE 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 MIP 1A MOUSE ?
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 :
CTLA 4 HumanDescription:
Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant
GSE, CD152, IDDM12, CELIAC3, CTLA-4.
Product # :
CYT-366Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- Citations
Description
CTLA 4 Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (36-161) and having a molecular mass of 15.9 kDa.CTLA 4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTLA 4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.
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Synonyms
GSE, CD152, IDDM12, CELIAC3, CTLA-4.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSD.
-
Background
Title: Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant: A Potential Immunotherapeutic Target
Abstract:
Cytotoxic T-lymphocyte associated antigen-4 (CTLA-4) is a key immune checkpoint receptor that plays a crucial role in regulating T-cell responses. This research paper provides an in-depth analysis of human recombinant CTLA-4, focusing on its production, characterization, and potential applications in immunotherapy. The paper discusses the significance of CTLA-4 in immune regulation, tumor immunity, and autoimmune diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CTLA-4 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CTLA-4 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Cytotoxic T-lymphocyte associated antigen-4 (CTLA-4) is a cell surface receptor primarily expressed on T-cells. It functions as a negative regulator of T-cell activation, dampening immune responses to prevent excessive inflammation. Human recombinant CTLA-4, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.Production and Characterization:
Recombinant CTLA-4 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CTLA-4.Role in Immune Regulation:
CTLA-4 plays a critical role in immune regulation by downregulating T-cell activation and suppressing immune responses. It competes with the co-stimulatory receptor CD28 for binding to its ligands, CD80 and CD86, on antigen-presenting cells. This interaction inhibits T-cell activation and promotes immune tolerance. Recombinant CTLA-4 serves as a valuable tool for studying immune checkpoint mechanisms and their impact on immune responses.Therapeutic Implications:
The blockade of CTLA-4 has emerged as a promising immunotherapeutic strategy in cancer treatment. Monoclonal antibodies targeting CTLA-4, such as ipilimumab, have shown significant clinical efficacy in enhancing anti-tumor immune responses. Recombinant CTLA-4-based therapies, including fusion proteins and engineered T-cell receptors, are being explored as potential immunotherapeutic interventions. Additionally, CTLA-4 plays a role in autoimmune diseases, making it a potential target for the development of novel treatments.Conclusion:
Human recombinant CTLA-4 is a valuable research tool and a potential immunotherapeutic target. Its production, characterization, and applications in immune regulation contribute to our understanding of T-cell biology and the development of novel immunotherapies. Continued research and clinical trials investigating the therapeutic potential of recombinant CTLA-4 offer promising prospects for improving outcomes in cancer and autoimmune diseases.What is the molecular weight/Mw of CTLA4 Protein?
CTLA4 Protein has a total Mw of 15.9kDa.
What is the source or expression system of CTLA4 Protein?
Escherichia Coli.
What is the Purity of CTLA4 Protein?
CTLA4 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CTLA4 Protein?
The biological functionality of CTLA4 Protein will be determined in the future.
What is the amino acid sequence of CTLA4 Protein?
MGSSHHHHHH SSGLVPRGSH MGSKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSD.
What applications can CTLA4 Protein be used in?
CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTLA4 Protein?
The endotoxin level is minimal, CTLA4 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 :
ANXA13 HumanDescription:
Annexin A13 Human Recombinant
Annexin A13, Annexin XIII, Annexin-13, Intestine-specific annexin, ISA, ANXA13, ANX13, MGC150460.
Product # :
PRO-197Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
- purity
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Description
ANXA13 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 336 amino acids (1-316 a.a.) and having a molecular mass of 37.5kDa. The ANXA13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 0.1M NaCl and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Annexin A13 (ANXA13) belongs to the annexin protein family, whose members play a role in cytoskeletal interactions, phospholipase inhibition, regulation of cellular growth, and intracellular signal transduction pathways. ANXA13 is believed to be the original originator of the 12 members of vertebrate annexins. ANXA13 expression is decidedly tissue-specific, being expressed only in intestinal and kidney epithelial cells. This expression is linked with a highly differentiated intracellular transport function.
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Synonyms
Annexin A13, Annexin XIII, Annexin-13, Intestine-specific annexin, ISA, ANXA13, ANX13, MGC150460.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGNRHAKASS PQGFDVDRDA KKLNKACKGM GTNEAAIIEI LSGRTSDERQ QIKQKYKATY GKELEEVLKS ELSGNFEKTA LALLDRPSEY AARQLQKAMK GLGTDESVLI EVLCTRTNKE IIAIKEAYQR LFDRSLESDV KGDTSGNLKK ILVSLLQANR NEGDDVDKDL AGQDAKDLYD AGEGRWGTDE LAFNEVLAKR SYKQLRATFQ AYQILIGKDI EEAIEEETSG DLQKAYLTLV RCAQDCEDYF AERLYKSMKG AGTDEETLIR IVVTRAEVDL QGIKAKFQEK YQKSLSDMVR SDTSGDFRKL LVALLH.
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 :
CXCL7 HumanDescription:
Neutrophil Activating Protein-2 Human Recombinant (CXCL7)
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Product # :
CHM-274Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Neutrophil Activating Protein-2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The NAP-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL7 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Purity
Greater than 97% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.sds-page
Citations
More Info
-
Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
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Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7should 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 Neutrophil Activating Protein-2in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.
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Background
What is the molecular weight/Mw of CXCL7 HUMAN Protein?
CXCL7 HUMAN Protein has a total Mw of 7.6kDa.
What is the source or expression system of CXCL7 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL7 HUMAN Protein?
CXCL7 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL7 HUMAN Protein?
The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CXCL7 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.
What applications can CXCL7 HUMAN Protein be used in?
CXCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL7 HUMAN Protein?
The endotoxin level is minimal, CXCL7 HUMAN Protein was purified using conventional chromatography techniques.Who supplies recombinant CXCL7 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 CXCL7 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 :
SHH MouseDescription:
Sonic Hedgehog Mouse Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein.
Product # :
CYT-597Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Sonic Hedgehog Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8 kDa. The Mouse Sonic Hedgehog is 99% homologous to the human gene.Cysteine at position 25 has been substituted with Ile.The Sonic HedgeHog is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 10mM Na2PO4 pH-7.5.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Determined by the dose-dependent induction of alkaline phosphatase production by C3H/10T1/2 (CCL-226) fibroblasts and is typically 0.48-0.72 µg/ml.Citations
More Info
-
Introduction
Recombinant Mouse Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Mouse Sonic Hedgehog is 99% homologous to the human gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Mouse Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Sonic Hedgehog 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
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG.
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 :
DSTN HumanDescription:
Destrin Human Recombinant
Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.
Product # :
PRO-1137Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DSTN Human Recombinant produced in E. coli is a single polypeptide chain containing 173 amino acids (1-165) and having a molecular mass of 19.5 kDa.DSTN is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DSTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Actin depolymerizing factor (Destrin/DSTN) belongs to the ADF/Cofilin/destrin superfamily which has the ability to swiftly depolymerize F-Actin in a stoichiometric mode. The ADF family of proteins is responsible for enhancing the turnover rate of actin in vivo. Destrin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. DSTN functions in a pH-independent manner. DSTN is found in a variety of epithelial and endothelial cells, however it is virtually nonexistent in adult mouse heart and skeletal muscle cells. Destrin shares a 71% sequence homology with Cofilin, however the 2 proteins vary in their interaction with Actin.
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Synonyms
Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.
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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.
-
Amino Acid Sequence
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPVLEHHH 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.
- View Data Sheet
Name :
IFNG Mouse, HisDescription:
Interferon-gamma Mouse Recombinant, His Tag
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-1001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- Citations
Description
Interferon-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (23-155a.a.) and having a molecular mass of 18.2kDa.IFNG is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IFNG protein solution (0.5mg/ml) containing 20mM MES buffer (pH5.0), 1mM DTT, 0.2M NaCl & 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. -
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered 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 MGSHMHGTVI ESLESLNNYF NSSGIDVEEK SLFLDIWRNW QKDGDMKILQ SQIISFYLRL FEVLKDNQAI SNNISVIESH LITTFFSNSK AKKDAFMSIA KFEVNNPQVQ RQAFNELIRV VHQLLPESSL RKRKRSRC.
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Background
What is the molecular weight/Mw of IFNG MOUSE, HIS Protein?
IFNG MOUSE, HIS Protein has a total Mw of 18.2kDa.
What is the source or expression system of IFNG MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of IFNG MOUSE, HIS Protein?
IFNG MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG MOUSE, HIS Protein?
The biological functionality of IFNG MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of IFNG MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMHGTVI ESLESLNNYF NSSGIDVEEK SLFLDIWRNW QKDGDMKILQ SQIISFYLRL FEVLKDNQAI SNNISVIESH LITTFFSNSK AKKDAFMSIA KFEVNNPQVQ RQAFNELIRV VHQLLPESSL RKRKRSRC.
What applications can IFNG MOUSE, HIS Protein be used in?
IFNG MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG MOUSE, HIS Protein?
The endotoxin level is minimal, IFNG MOUSE, HIS 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 :
OSR2 HumanDescription:
Odd-Skipped Related Transcription Factor 2 Human Recombinant
Odd-Skipped Related Transcription Factor 2 , Odd-Skipped Related 2 (Drosophila), Protein odd-skipped-related 2.
Product # :
PRO-2067Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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Description
OSR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a) and having a molecular mass of 33kDa. OSR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
OSR2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Odd-Skipped Related Transcription Factor 2, also know as OSR2 belongs to the Odd C2H2-type zinc-finger protein family. OSR2 is a mammalian homolog of the Drosophila odd-skipped family of transcription factors.
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Synonyms
Odd-Skipped Related Transcription Factor 2 , Odd-Skipped Related 2 (Drosophila), Protein odd-skipped-related 2.
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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 MGSMGSKALP APIPLHPSLQ LTNYSFLQAV NTFPATVDHL QGLYGLSAVQ TMHMNHWTLG YPNVHEITRS TITEMAAAQG LVDARFPFPA LPFTTHLFHP KQGAIAHVLP ALHKDRPRFD FANLAVAATQ EDPPKMGDLS KLSPGLGSPI SGLSKLTPDR KPSRGRLPSK TKKEFICKFC GRHFTKSYNL LIHERTHTDE RPYTCDICHK AFRRQDHLRD HRYIHSKEKP FKCQECGKGF CQSRTLAVHK TLHMQTSSPT AASSAAKCSG ETVICGGTA.
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 :
CX3CL1 MouseDescription:
Fractalkine Mouse Recombinant (CX3CL1)
Fractalkine, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1, Cx3cl1, Cx3c, Fkn, Scyd1, CX3C, ABCD-3, AB030188, AI848747, D8Bwg0439e.
Product # :
CHM-017Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
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- biological activity
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Description
Fractalkine Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa. The CX3CL1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 µg/ml, corresponding to a specific activity of > 2000IU/mg.Citations
More Info
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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1, Cx3cl1, Cx3c, Fkn, Scyd1, CX3C, ABCD-3, AB030188, AI848747, D8Bwg0439e.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CX3CL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CX3CL1 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 CX3CL1 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
QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG.
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Background
What is the molecular weight/Mw of CX3CL1 MOUSE Protein?
CX3CL1 MOUSE Protein has a total Mw of 8.7kDa.
What is the source or expression system of CX3CL1 MOUSE Protein?
Escherichia Coli.
What is the Purity of CX3CL1 MOUSE Protein?
CX3CL1 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 MOUSE Protein?
The ED50as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 µg/ml, corresponding to a specific activity of > 2000IU/mg.
What is the amino acid sequence of CX3CL1 MOUSE Protein?
QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG.
What applications can CX3CL1 MOUSE Protein be used in?
CX3CL1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 MOUSE Protein?
The endotoxin level is minimal, CX3CL1 MOUSE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CX3CL1 MOUSE 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 CX3CL1 MOUSE?
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 :
GCHFR HumanDescription:
GTP Cyclohydrolase I Feedback Regulator Human Recombinant
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
Product # :
PRO-2006Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
- purity
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Description
GCHFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 107 amino acids (1-84a.a) and having a molecular mass of 12.1kDa. GCHFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GCHFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GTP Cyclohydrolase I Feedback Regulator, also known as GCHFR, is a Protein coding gene which includes a homodimer. GCHFR binds and mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase I. GCHFR also regulates phenylalanine metabolism in the liver and in the production of biogenic amine neurotransmitters and nitric oxide.
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Synonyms
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
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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 MGSMPYLLIS TQIRMEVGPT MVGDEQSDPE LMQHLGASKR RALGNNFYEY YVDDPPRIVL DKLERRGFRV LSMTGVGQTL VWCLHKE.
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 :
GCSAM HumanDescription:
Germinal Center-Associated, Signaling and Motility Human Recombinant
GCAT2, HGAL, Germinal center-associated signaling and motility protein, Germinal center B-cell-expressed transcript 2 protein, Germinal center-associated lymphoma protein, GAL, GCET2 .
Product # :
PRO-1282Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GCSAM Human Recombinant produced in E. coli is a single polypeptide chain containing 201 amino acids (1-178) and having a molecular mass of 23 kDa. GCSAM is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GCSAM solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GCSAM is a protein which functions in signal transduction pathways and whose expression raises in germinal cell lymphomas. GCSAM contains a putative PDZ-interacting domain, an immunoreceptor tyrosine-based activation motif (ITAM), and two putative SH2 binding sites. In B cells, GCSAM expression is particularly induced by interleukin-4.
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Synonyms
GCAT2, HGAL, Germinal center-associated signaling and motility protein, Germinal center B-cell-expressed transcript 2 protein, Germinal center-associated lymphoma protein, GAL, GCET2 .
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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 MGSMGNSLLR ENRRQQNTQE MPWNVRMQSP KQRTSRCWDH HIAEGCFCLP WKKILIFEKR QDSQNENERM SSTPIQDNVD QTYSEELCYT LINHRVLCTR PSGNSAEEYY ENVPCKAERP RESLGGTETE YSLLHMPSTD PRHARSPEDE YELLMPHRIS SHFLQQPRPL MAPSETQFSH L.
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 :
S100A8 MouseDescription:
S100 Calcium Binding Protein A8 Mouse Recombinant
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-233Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A8 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89a.a) and having a molecular mass of 12.4kDa.S100A8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A8 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
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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 MPSELEKALS NLIDVYHNYS NIQGNHHALY KNDFKKMVTT ECPQFVQNIN IENLFRELDI NSDNAINFEE FLAMVIKVGV ASHKDSHKE
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 :
HDHD1 HumanDescription:
Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 Human Recombinant
Pseudouridine-5'-monophosphatase, 5'-PsiMPase, Haloacid dehalogenase-like hydrolase domain-containing protein 1, Haloacid dehalogenase-like hydrolase domain-containing protein 1A, Protein GS1, HDHD1, DXF68S1E, FAM16AX, GS1, HDHD1A.
Product # :
ENZ-028Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HDHD1 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 248 amino acids (1-228 a.a.) and having a molecular mass of 27.4kDa. The HDHD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HDHD1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol,
0.1M NaCl and 1mM DTT.Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Haloacid dehalogenase-like hydrolase domain-containing protein 1A (HDHD1A) is a member of the adiponutrin family. HDHD1A is interesting because it is an X-linked gene that escapes X-inactivation. HDHD1A is particularly important in the perception of human X chromosome structural organization as well as the mechanism of X-inactivation.
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Synonyms
Pseudouridine-5'-monophosphatase, 5'-PsiMPase, Haloacid dehalogenase-like hydrolase domain-containing protein 1, Haloacid dehalogenase-like hydrolase domain-containing protein 1A, Protein GS1, HDHD1, DXF68S1E, FAM16AX, GS1, HDHD1A.
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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 MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM GKKALEAAQI IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII HLRKHGIPFA LATSSGSASF DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP DPDIFLACAK RFSPPPAMEK CLVFEDAPNG VEAALAAGMQ VVMVPDGNLS RDLTTKATLV LNSLQDFQPE LFGLPSYE.
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.