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1000 results found for “glucagon”
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Name :
PTH (7-84) HumanDescription:
Parathyroid Hormone (7-84) Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-011Price :
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Description
PTH (7-84) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids, having an MW of 8.8kDa. The PTH (7-84) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2 µm 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.Citations
More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
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Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PTH (7-84) although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTH (7-84) should be stored at 4C between 2-7 days and for future use below -18C.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 PTH (7-84) in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ.
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 :
SPA-CysDescription:
Staphylococcal Protein-A Cys Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1922Price :
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Description
SPA-Cys Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with a Cys on C-terminus. SPA-Cys is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 297 amino acids and having a molecular mass of 33.5kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by: (a) Analysis by HPLC.(b) Analysis by SDS-PAGE.
Citations
More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDC
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 :
HPSE WBDescription:
Recombinant Human Heparanase-1 WB Control
Product # :
ENZ-261Price :
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Description
Recombinant Heparanase protein HPA1 is produced in CHO cells.The protein is purified by several orthogonal chromatography steps.
Formulation
Concentration: 1μg /ml
Content: 100 ng
Buffer: LDS-PAGE buffer
[140 mM Tris buffer pH 8.5, 10% Glycerol, 2% LDS, 0.015% EDTA, 1.88% (v/v) of 1% Serva Blue G250 and 0.625% (v/v) of 1% Phenol red].Citations
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Introduction
Heparanase is an endo β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).
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Applications
Positive control for western blot analysis.
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Preparation protocol
Use 20 μl of recombinant human heparanase 1 (HPA1) per lane, as a control for using monoclonal anti HPA 1 clone HP3/17 antibodies (Cat. No.: Ins-AB-04001) or polyclonal rabbit anti HPA1 antibody (Cat. No.: Ins-AB-04002).
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Data Sheet
To view the FULL VERSION data sheet click Heparanase-1 WB Protein:
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Storage Procedures
Store at –20ºC, avoid repeated freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GLA HumanDescription:
Alpha-Galactosidase Human Recombinant
Alpha-galactosidase A, Alpha-D-galactosidase A, Alpha-D-galactoside galactohydrolase, Melibiase, GLA, GALA.
Product # :
ENZ-926Price :
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Description
GLA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (32-429 a.a.) and having a molecular mass of 46.4kDa GLA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GLA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alpha-galactosidase A (GLA) is a homodimeric glycoprotein which hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. GLA catalyzes the hydrolysis of melibiose into galactose and glucose. Various mutations in the GLA gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease (a rare lysosomal storage disorder which results from a failure to catabolize alpha-D-galactosyl glycolipid moieties).
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Synonyms
Alpha-galactosidase A, Alpha-D-galactosidase A, Alpha-D-galactoside galactohydrolase, Melibiase, GLA, GALA.
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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
LDNGLARTPT MGWLHWERFM CNLDCQEEPD SCISEKLFME MAELMVSEGW KDAGYEYLCI DDCWMAPQRD SEGRLQADPQ RFPHGIRQLA NYVHSKGLKL GIYADVGNKT CAGFPGSFGY YDIDAQTFAD WGVDLLKFDG CYCDSLENLA DGYKHMSLAL NRTGRSIVYS CEWPLYMWPF QKPNYTEIRQ YCNHWRNFAD IDDSWKSIKS ILDWTSFNQE RIVDVAGPGG WNDPDMLVIG NFGLSWNQQV TQMALWAIMA APLFMSNDLR HISPQAKALL QDKDVIAINQ DPLGKQGYQL RQGDNFEVWE RPLSGLAWAV AMINRQEIGG PRSYTIAVAS LGKGVACNPA CFITQLLPVK RKLGFYEWTS RLRSHINPTG TVLLQLENTM QMSLKDLLVE HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FCER1A Human, HEKDescription:
Fc-Epsilon RI-Alpha Human Recombinant, HEK
FCERIA, FCERA, Fc epsilon receptor Ia, Fcepsilon RI-alpha, Fc epsilon RI alpha chain, FcERI, High affinity immunoglobulin epsilon receptor subunit alpha isoform1, IgE Fc receptor subunit alpha, FCER1A, FCE1A.
Product # :
PRO-2779Price :
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Description
FCER1A Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 186 amino acids (26-205aa) and having a molecular mass of 21.8kDa. FCER1A is fused to a 6 His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293.
Formulation
FCER1A protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 0.01 ug/ml and is measured by its binding ability in a functional ELISA with Human IgE.
Citations
More Info
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Synonyms
FCERIA, FCERA, Fc epsilon receptor Ia, Fcepsilon RI-alpha, Fc epsilon RI alpha chain, FcERI, High affinity immunoglobulin epsilon receptor subunit alpha isoform1, IgE Fc receptor subunit alpha, FCER1A, FCE1A.
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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
VPQKPKVSLN PPWNRIFKGE NVTLTCNGNN FFEVSSTKWF HNGSLSEETN SSLNIVNAKF EDSGEYKCQH QQVNESEPVY LEVFSDWLLL QASAEVVMEG QPLFLRCHGW RNWDVYKVIY YKDGEALKYW YENHNISITN ATVEDSGTYY CTGKVWQLDY ESEPLNITVI KAPREKYWLQ HHHHHH
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Background
The FCER1A gene encodes the alpha subunit of the high-affinity immunoglobulin E (IgE) receptor, known as FCER1A. This receptor is primarily expressed on mast cells and basophils, and its activation plays a pivotal role in allergic and inflammatory responses. This research aims to explore the significance of FCER1A and its potential implications in allergic disorders and immune-mediated diseases. By investigating the functions and regulation of FCER1A, we can gain insights into its role in immune responses and identify potential therapeutic targets.
The FCER1A receptor is responsible for the binding of IgE antibodies, initiating a cascade of signaling events upon allergen exposure. Crosslinking of IgE-bound FCER1A leads to the release of various inflammatory mediators, such as histamine, cytokines, and leukotrienes, which contribute to the clinical manifestations of allergic reactions. Understanding the molecular mechanisms underlying FCER1A activation and downstream signaling is crucial for comprehending allergic diseases.
In addition to its role in allergies, FCER1A has been implicated in immune-mediated inflammatory diseases, including asthma, atopic dermatitis, and autoimmune conditions. Dysregulation of FCER1A expression and signaling pathways can lead to exaggerated immune responses and chronic inflammation. Investigating the genetic and epigenetic factors influencing FCER1A expression and the interplay between FCER1A and other immune molecules can provide valuable insights into disease pathogenesis.
This research will delve into the molecular mechanisms governing FCER1A expression, activation, and downstream signaling pathways. The paper will explore the regulatory effects of FCER1A on mast cell and basophil activation, the release of inflammatory mediators, and the recruitment of other immune cells. Additionally, it will examine the impact of FCER1A dysregulation in allergic and immune-mediated diseases and discuss the potential of FCER1A as a therapeutic target for intervention.
The study will also investigate the diagnostic and prognostic value of FCER1A in various allergic and immune disorders. Understanding the expression patterns and alterations of FCER1A in different diseases and patient populations may aid in disease stratification, treatment selection, and monitoring of treatment response.
By unraveling the molecular mechanisms underlying FCER1A's functions in allergic and inflammatory responses, this research aims to contribute to our understanding of immune-mediated diseases. Furthermore, it highlights the potential of FCER1A as a target for therapeutic interventions and emphasizes the need for further investigations to develop novel treatments and improve patient outcomes.
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 :
LRG1 Human, Sf9Description:
Leucine-Rich Alpha-2-Glycoprotein 1 Human Recombinant, Sf9
Leucine Rich Alpha-2-Glycoprotein 1, Leucine-Rich Alpha-2-Glycoprotein, 1300008B03Rik, 2310031E04Rik, HMFT1766, Leucine-rich alpha-2-glycoprotein, LRG1, LRG.
Product # :
PRO-2530Price :
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Description
LRG1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 321 amino acids (36-347a.a.) and having a molecular mass of 35.4kDa. LRG1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LRG1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
LRG1 belongs to the leucine-rich repeat (LRR) family of proteins, which have been shown to be involved in protein-protein interaction, signal transduction, cell adhesion and development. The LRG1 is expressed during granulocyte differentiation.
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Synonyms
Leucine Rich Alpha-2-Glycoprotein 1, Leucine-Rich Alpha-2-Glycoprotein, 1300008B03Rik, 2310031E04Rik, HMFT1766, Leucine-rich alpha-2-glycoprotein, LRG1, LRG.
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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
ADPVTLSPKD CQVFRSDHGS SISCQPPAEI PGYLPADTVH LAVEFFNLTH LPANLLQGAS KLQELHLSSN GLESLSPEFL RPVPQLRVLD LTRNALTGLP PGLFQASATL DTLVLKENQL EVLEVSWLHG LKALGHLDLS GNRLRKLPPG LLANFTLLRT LDLGENQLET LPPDLLRGPL QLERLHLEGN KLQVLGKDLL LPQPDLRYLF LNGNKLARVA AGAFQGLRQL DMLDLSNNSL ASVPEGLWAS LGQPNWDMRD GFDISGNPWI CDQNLSDLYR WLQAQKDKMF SQNDTRCAGP EAVKGQTLLA VAKSQHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ITGB3BP HumanDescription:
Integrin Beta 3 Binding Protein Human Recombinant
CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.
Product # :
PRO-1435Price :
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Description
ITGB3BP Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 27.1kDa. ITGB3BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ITGB3BP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.
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Synonyms
CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.
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Physical Appearance
Sterile Filtered colorless solution.
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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 MGSMPFAPVA QARVQWHDFR SLQHLLPAFK RFSCLSLGSS WDYSVKRSLK LDGLLEENSF DPSKITRKKS VITYSPTTGT CQMSLFASPT SSEEQKHRNG LSNEKRKKLN HPSLTESKES TTKDNDEFMM LLSKVEKLSE EIMEIMQNLS SIQALEGSRE LENLIGISCA SHFLKREMQK TKELMTKVNK QKLFEKSTGL PHKASRHLDS YEFLKAILN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GLO1 MouseDescription:
Glyoxalase-I Mouse Recombinant
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
Product # :
ENZ-953Price :
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Description
GLO1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 192 amino acids (1-184a.a.) and having a molecular mass of 21.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GLO1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GLO1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 210 units/mg, and is defined as the amount of enzyme that will form 1.0 µmol of S-lactoylglutathione from methylglyoxal and reduced glutathione per minute at pH 6.5 at 25C.Citations
More Info
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Introduction
GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.
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Synonyms
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
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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
MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATIILEHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TriptorelinDescription:
Triptorelin Acetate
Product # :
HOR-238Price :
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Shipped at Room temp
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Description
Triptorelin C64H82N18O13, Pyr-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-Gly-NH2 is a synthetic analogue of gonadorelin (GnRH). As a result of the substitution of the 6th amino acid residue in the native molecule, the agonistic effect is more pronounced and the plasma half-life prolonged.
Formulation
The protein (1 mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Trp although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Trp should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Trp in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the Purity of TRIPTORELIN Protein?
TRIPTORELIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of TRIPTORELIN Protein?
The biological functionality of TRIPTORELIN Protein will be determined in the future.
What applications can TRIPTORELIN Protein be used in?
TRIPTORELIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TRIPTORELIN Protein?
The endotoxin level is minimal, TRIPTORELIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Ag85BDescription:
Mycobacterium Tuberculosis major secretory protein Antigen 85B Recombinant
Antigen 85-B, 85B, Extracellular alpha-antigen, Antigen 85 complex B, Ag85B, Mycolyl transferase 85B, EC 2.3.1.-, Fibronectin-binding protein B, 30 kDa extracellular protein, fbpB, A85B, Major Secretory Protein Antigen 85B.
Product # :
PRO-589Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ag85B Recombinant His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 30kDa.
Source
Escherichia Coli.
Formulation
Lyophilized with no additives.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Antigen 85B Mycobacterium Tuberculosis-is the most abundant protein exposed by M. Tuberculosis, as well as a potent immunoprotective antigen and a leading drug target. Ag85 induces strong T-cell proliferation and IFN-g secretion in most healthy individuals exposed to M. tuberculosis, in BCG-vaccinated mice and humans, whereas the antibody against Ag85 are more prevalent in active tuberculosis patients with decreased cellular immune response.
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Synonyms
Antigen 85-B, 85B, Extracellular alpha-antigen, Antigen 85 complex B, Ag85B, Mycolyl transferase 85B, EC 2.3.1.-, Fibronectin-binding protein B, 30 kDa extracellular protein, fbpB, A85B, Major Secretory Protein Antigen 85B.
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Physical Appearance
Sterile Filtered and lyophilized, though might appear as a solution as a result of the glycerol content.
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Stability
Ag85B although stable room temperature for 4 weeks, should be stored desiccated 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 Antigen-85B 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
MRGSHHHHHHFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQ
DDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETF
LTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDP
SQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVY
CGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWE
YWGAQLNAMKGDLQSSLGAG.
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 :
CXCL9 BovineDescription:
MIG (CXCL9) Bovine Recombinant
Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.
Product # :
CHM-041Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MIG (CXCL9) BovineRecombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 104 amino acids and having a molecular mass of approximately 18.0kDa.MIG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.
Citations
More Info
-
Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belongs to the CXC chemokine family that is also known as Monokine induced by gamma INF (MIG). CXCL9 is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
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Synonyms
Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIG (CXCL9) 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 MIG (CXCL9) 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
VPAIRNGRCS CINTSQGMIH PKSLKDLKQF APSPSCEKTE IIATMKNGNE ACLNPDLPEV KELIKEWEKQ VNQKKKQRKG KKYKKTKKVP KVKRSQRPSQ KKTT.
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Background
What is the molecular weight/Mw of CXCL9 BOVINE Protein?
CXCL9 BOVINE Protein has a total Mw of 18kDa.
What is the source or expression system of CXCL9 BOVINE Protein?
Escherichia Coli.
What is the Purity of CXCL9 BOVINE Protein?
CXCL9 BOVINE Protein is > 96% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL9 BOVINE Protein?
The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.
What is the amino acid sequence of CXCL9 BOVINE Protein?
VPAIRNGRCS CINTSQGMIH PKSLKDLKQF APSPSCEKTE IIATMKNGNE ACLNPDLPEV KELIKEWEKQ VNQKKKQRKG KKYKKTKKVP KVKRSQRPSQ KKTT.
What applications can CXCL9 BOVINE Protein be used in?
CXCL9 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL9 BOVINE Protein?
The endotoxin level is minimal, CXCL9 BOVINE 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 :
S100A10 HumanDescription:
S100 Calcium Binding Protein A10 Human Recombinant
Protein S100-A10, S100 calcium-binding protein A10, Calpactin-1 light chain, Calpactin I light chain, p10 protein, p11, Cellular ligand of annexin II, S100A10, ANX2LG, CAL1L, CLP11, 42C, p10, GP11, ANX2L, Ca[1], MGC111133.
Product # :
PRO-384Price :
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Description
S100A10 Human Recombinant also called Calpactin light chain is expressed in E. coli having a molecular weight of 15.3kDa fused to an amino terminal hexahistidine tag.
Source
Escherichia Coli.
Formulation
S100-A10 is supplied in 1xPBS and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
2 bands on Western blot at 15.3 and 30.6 kDa, respectively representing monomeric and dimeric form.Citations
More Info
-
Introduction
S100A10 is a member of the S100 family of proteins contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A10 may function in exocytosis and endocytosis.
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Synonyms
Protein S100-A10, S100 calcium-binding protein A10, Calpactin-1 light chain, Calpactin I light chain, p10 protein, p11, Cellular ligand of annexin II, S100A10, ANX2LG, CAL1L, CLP11, 42C, p10, GP11, ANX2L, Ca[1], MGC111133.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Applications
S100A10 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.
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 :
Activin A Human PlantDescription:
Activin A Human Recombinant, Plant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-052Price :
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Shipped at Room temp
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Description
Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
Citations
More Info
-
Introduction
Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Activin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin A 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 Activin A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.
What is the source or expression system of Activin A Protein?
Nicotinia
What is the Purity of Activin A Protein?
Activin A Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological functionality of Activin-A Protein will be determined in the future.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
-
Serological Identification
The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.
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 :
AKR1C4 HumanDescription:
Aldo-Keto Reductase Family 1 Member C4 Human Recombinant
Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.
Product # :
ENZ-1132Price :
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Description
AKR1C4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 323 amino acids (1-323aa ) and having a molecular mass of 37kDa.
Source
Escherichia Coli.
Formulation
AKR1C4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 700pmol/min/ug, and is defined as the amount of enzyme that catalyze the oxidation of 1.0pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25C
Citations
More Info
-
Introduction
Aldo-keto reductase family 1 member C4 or AKR1C4 is a part of the aldo/keto reductase superfamily that has more then 40 known proteins & enzymes. AKR1C4 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols with NADH and/or NADPH as cofactors. AKR1C4 takes place in the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in the liver tissue.
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Synonyms
Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.
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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
MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID SAYLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE SSLKKLQLDY VDLYLLHFPM ALKPGETPLP KDENGKVIFD TVDLSATWEV MEKCKDAGLA KSIGVSNFNC RQLEMILNKP GLKYKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN RNYRYVVMDF LMDHPDYPFS DEY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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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
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH 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.
- View Data Sheet
Name :
SLC3A2 HumanDescription:
Solute Carrier Family 3 Member 2 Human Recombinant
Solute Carrier Family 3 Member 2, Lymphocyte Activation Antigen 4F2 Large Subunit, Solute Carrier Family 3 (Activators Of Dibasic And Neutral Amino Acid Transport), Member 2, Antigen Identified By Monoclonal Antibodies 4F2, TRA1.10, TROP4, And T43, Solute Carrier Family 3 (Amino Acid Transporter Heavy Chain), Member 2, 4F2 Cell-Surface Antigen Heavy Chain, Monoclonal Antibody 44D7, CD98 Heavy Chain, 4F2HC, MDU1, Antigen Defined By Monoclonal Antibody 4F2, Heavy Chain, Antigen Defined By Monoclonal Antibody 4F2, 4F2 Heavy Chain Antigen, 4F2 Heavy Chain, CD98 Antigen, Heavy Chain, CD98HC, 4T2HC, NACAE, CD98, 4F2, 4F2 cell-surface antigen heavy chain.
Product # :
PRO-2489Price :
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Description
SLC3A2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (206-630a.a.) and having a molecular mass of 47.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).SLC3A2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SLC3A2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
SLC3A2, also known as Solute Carrier Family 3 Member 2, is a single-pass type II membrane protein which is part of the SLC3A transporter family. SLC3A2 is expressed ubiquitously in all tissues tested with the highest levels detected in kidney, placenta and testis and lowest level in thymus. SLC3A2 is essential for the function of light chain amino-acid transporters and also takes part in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. SLC3A2 participates in guiding and targeting of LAT1 and LAT2 to the plasma membrane.
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Synonyms
Solute Carrier Family 3 Member 2, Lymphocyte Activation Antigen 4F2 Large Subunit, Solute Carrier Family 3 (Activators Of Dibasic And Neutral Amino Acid Transport), Member 2, Antigen Identified By Monoclonal Antibodies 4F2, TRA1.10, TROP4, And T43, Solute Carrier Family 3 (Amino Acid Transporter Heavy Chain), Member 2, 4F2 Cell-Surface Antigen Heavy Chain, Monoclonal Antibody 44D7, CD98 Heavy Chain, 4F2HC, MDU1, Antigen Defined By Monoclonal Antibody 4F2, Heavy Chain, Antigen Defined By Monoclonal Antibody 4F2, 4F2 Heavy Chain Antigen, 4F2 Heavy Chain, CD98 Antigen, Heavy Chain, CD98HC, 4T2HC, NACAE, CD98, 4F2, 4F2 cell-surface antigen heavy chain.
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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
ADPRAPRCRE LPAQKWWHTG ALYRIGDLQA FQGHGAGNLA GLKGRLDYLS SLKVKGLVLG PIHKNQKDDV AQTDLLQIDP NFGSKEDFDS LLQSAKKKSI RVILDLTPNY RGENSWFSTQ VDTVATKVKD ALEFWLQAGV DGFQVRDIEN LKDASSFLAE WQNITKGFSE DRLLIAGTNS SDLQQILSLL ESNKDLLLTS SYLSDSGSTG EHTKSLVTQY LNATGNRWCS WSLSQARLLT SFLPAQLLRL YQLMLFTLPG TPVFSYGDEI GLDAAALPGQ PMEAPVMLWD ESSFPDIPGA VSANMTVKGQ SEDPGSLLSL FRRLSDQRSK ERSLLHGDFH AFSAGPGLFS YIRHWDQNER FLVVLNFGDV GLSAGLQASD LPASASLPAK ADLLLSTQPG REEGSPLELE RLKLEPHEGL LLRFPYAAHH 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 :
CANT1 HumanDescription:
Calcium Activated Nucleotidase 1 Human Recombinant
Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.
Product # :
PRO-1010Price :
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Description
CANT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (63-401 a.a.) and having a molecular mass of 40.5kDa. CANT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CANT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.
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Synonyms
Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.
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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 MGSHMRPAPG RPPTHNAHNW RLGQAPANWY NDTYPLSPPQ RTPAGIRYRI AVIADLDTES RAQEENTWFS YLKKGYLTLS DSGDKVAVEW DKDHGVLESH LAEKGRGMEL SDLIVFNGKL YSVDDRTGVV YQIEGSKAVP WVILSDGDGT VEKGFKAEWL AVKDERLYVG GLGKEWTTTT GDVVNENPEW VKVVGYKGSV DHENWVSNYN ALRAAAGIQP PGYLIHESAC WSDTLQRWFF LPRRASQERY SEKDDERKGA NLLLSASPDF GDIAVSHVGA VVPTHGFSSF KFIPNTDDQI IVALKSEEDS GRVASYIMAF TLDGRFLLPE TKIGSVKYEG IEFI.
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 :
PGAM2 Human, ActiveDescription:
Phosphoglycerate Mutase 2 Human Recombinant, Active
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
Product # :
ENZ-981Price :
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Description
PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGAM2 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.
Biological Activity
Specific activity is > 100units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C.Citations
More Info
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Introduction
Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.
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Synonyms
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
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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 MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.
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 :
TGM2 Human, Sf9Description:
Tissue Transglutaminase Human Recombinant, Sf9
Protein-glutamine gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.
Product # :
ENZ-303Price :
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Description
Tissue Transglutaminase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 83 kDa. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.
Source
Sf9 insect cells.
Formulation
TGM2 is supplied in 16mM HEPES buffer pH-8.0, 320mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins. -
Synonyms
Protein-glutamine gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.
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Stability
Store at 4°C if entire vial will be used within 2-4weeks. Store, frozen at -20°C for longer periods of time. 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.
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Name :
TIGIT HumanDescription:
T-Cell Immunoreceptor With Ig And ITIM Domains Human Recombinant
VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.
Product # :
PRO-2498Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TIGIT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 359 amino acids (22-141a.a.) and having a molecular mass of 40.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TIGIT is expressed with a 239 amino acid hlgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TIGIT protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
T cell immunoreceptor with Ig and ITIM domains or TIGIT, is an immune receptor located on part of T cells and Natural Killer Cells(NK). TIGIT is also known as Vstm3 and WUCAM. The receptor can bind with high affinity to dendritic cells(DCs), CD155(PVR) on macrophages, etc., and it can bind with lower affinity to CD112(PVRL2). TIGIT can inhibit the cytotoxicity of Natural Killer Cells through its ITIM domain via antibodies against the interaction with PVR and the activity is directed. It has been show on research that TIGIT-Fc fusion molecule can have interaction with PVR on dendritic cells and elevate its IL-10 secretion level or lower the secretion on IL-12 under the stimulation of LPS, moreover, it can inhibit the activation of T cell in vivo.
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Synonyms
VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MMTGTIETTG NISAEKGGSI ILQCHLSSTT AQVTQVNWEQ QDQLLAICNA DLGWHISPSF KDRVAPGPGL GLTLQSLTVN DTGEYFCIYH TYPDGTYTGR IFLEVLESSV AEHGARFQIP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.
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 :
KIAA0101 HumanDescription:
KIAA0101 Human Recombinant
KIAA0101, L5, NS5ATP9, OEATC, OEATC-1, OEATC1, p15(PAF), p15/PAF, p15PAF, PAF, PAF15, PCNA-associated factor, Hepatitis C virus NS5A-transactivated protein 9, HCV NS5A-transactivated protein 9, Overexpressed in anaplastic thyroid carcinoma 1, PCNA-associated factor of 15 kDa.
Product # :
PRO-1683Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KIAA0101 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-111) and having a molecular mass of 14.4 kDa.KIAA0101 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KIAA0101 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
KIAA0101 is a PCNA-binding protein which performs as a regulator of DNA repair all through DNA replication. Subsequent to DNA mutilation, the collaboration with PCNA is interrupted, enabling the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, assisting the bypass of replication-fork-blocking lesions. Additionally, KIAA0101 performs as a controller of centrosome number.
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Synonyms
KIAA0101, L5, NS5ATP9, OEATC, OEATC-1, OEATC1, p15(PAF), p15/PAF, p15PAF, PAF, PAF15, PCNA-associated factor, Hepatitis C virus NS5A-transactivated protein 9, HCV NS5A-transactivated protein 9, Overexpressed in anaplastic thyroid carcinoma 1, PCNA-associated factor of 15 kDa.
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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 MGSMVRTKAD SVPGTYRKVV AARAPRKVLG SSTSATNSTS VSSRKAENKY AGGNPVCVRP TPKWQKGIGE FFRLSPKDSE KENQIPEEAG SSGLGKAKRK ACPLQPDHTN DEKE.
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 :
G CSF Human, HisDescription:
Granulocyte-Colony Stimulating Factor Human Recombinant, His Tag
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-476Price :
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Shipping Method :
Shipped with Ice Packs
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Description
Granulocyte Colony Stimulating Factor-His Tag Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids, fragment (31-204) and having a molecular mass of 23.19 kDa with an amino-terminal hexahistidine tag.G-CSF-His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Granulocyte Colony Stimulating Factor His is supplied in 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of G CSF Protein?
G CSF Protein has a total Mw of 23.19kDa.
What is the source or expression system of G CSF Protein?
Escherichia Coli.
What is the Purity of G CSF Protein?
G CSF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF Protein?
The biological functionality of G CSF Protein will be determined in the future.
What is the amino acid sequence of G CSF Protein?
G CSF Protein is composed from 174 amino acids.
What applications can G CSF Protein be used in?
G CSF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF Protein?
The endotoxin level is minimal, G CSF 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 :
Procalcitonin CanineDescription:
Procalcitonin Canine Recombinant
Calcitonin, Calca, Calc, CCALCI.
Product # :
HOR-015Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Procalcitonin Canine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Arg130) containing 115 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 12.7kDa.
Source
Escherichia Coli.
Formulation
Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 7.2.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Calcitonin, Calca, Calc, CCALCI.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin 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
MKHHHHHHASAPFRSALEGL PDPTALSEKE GRLLLAALVK AYVQRKNELE QEQEQETEGS SLDSSRAKRC SNLSTCVLGT YSKDLNNFHT FSGIGFGAET PGKKRDIASG LERGR.
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 :
LGALS9 MouseDescription:
Galectin-9 Mouse Recombinant
Galectin-9, Gal-9, Lgals9, Lgals5, LGALS35, AA407335, AI194909, AI265545.
Product # :
CYT-550Price :
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Shipped with Ice Packs
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Description
LGALS9 mouse Recombinant produced E. coli is a single polypeptide chain containing 345 amino acids (1-322) and having a molecular mass of 38kDa.LGALS9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS9 solution (0.5mg/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.
SDS-PAGE
Citations
More Info
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Introduction
LGLAS9 binds galactosides and has high affinity for the Forssman pentasaccharide. LGLAS9 participates in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. LGLAS9 is a ligand for HAVCR2/TIM3. LGLAS9 Induces T-helper type 1 lymphocyte (Th1) death. LGLAS9 performs as an eosinophil chemoattractant LGLAS9 is an S-type lectin which is over-expressed in Hodgkin's disease tissue and takes part in the interaction between the H&RS cells with their surrounding cells.
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Synonyms
Galectin-9, Gal-9, Lgals9, Lgals5, LGALS35, AA407335, AI194909, AI265545.
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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 MGSMALFSAQ SPYINPIIPF TGPIQGGLQE GLQVTLQGTT KSFAQRFVVN FQNSFNGNDI AFHFNPRFEE GGYVVCNTKQ NGQWGPEERK MQMPFQKGMP FELCFLVQRS EFKVMVNKKF FVQYQHRVPY HLVDTIAVSG CLKLSFITFQ TQNFRPAHQA PMAQTTIHMV HSTPGQMFST PGIPPVVYPT PAYTIPFYTP IPNGLYPSKS IMISGNVLPD ATRFHINLRC GGDIAFHLNP RFNENAVVRN TQINNSWGQE ERSLLGRMPF SRGQSFSVWI ICEGHCFKVA VNGQHMCEYY HRLKNLQDIN TLEVAGDIQL THVQT.
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Background
What is the molecular weight/Mw of LGALS9 MOUSE Protein?
LGALS9 MOUSE Protein has a total Mw of 38kDa.
What is the source or expression system of LGALS9 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS9 MOUSE Protein?
LGALS9 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS9 MOUSE Protein?
The biological functionality of LGALS9 MOUSE Protein will be determined in the future.
What is the amino acid sequence of LGALS9 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMALFSAQ SPYINPIIPF TGPIQGGLQE GLQVTLQGTT KSFAQRFVVN FQNSFNGNDI AFHFNPRFEE GGYVVCNTKQ NGQWGPEERK MQMPFQKGMP FELCFLVQRS EFKVMVNKKF FVQYQHRVPY HLVDTIAVSG CLKLSFITFQ TQNFRPAHQA PMAQTTIHMV HSTPGQMFST PGIPPVVYPT PAYTIPFYTP IPNGLYPSKS IMISGNVLPD ATRFHINLRC GGDIAFHLNP RFNENAVVRN TQINNSWGQE ERSLLGRMPF SRGQSFSVWI ICEGHCFKVA VNGQHMCEYY HRLKNLQDIN TLEVAGDIQL THVQT.
What applications can LGALS9 MOUSE Protein be used in?
LGALS9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS9 MOUSE Protein?
The endotoxin level is minimal, LGALS9 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.