抗SP-D抗体(Anti-SP-D, Goat-Poly antibody)
掲載日情報：2018/11/26 現在Webページ番号：30479
SP-Dに対する抗体(Anti-SP-D, Goat-Poly )です。
※ 本製品は研究用です。研究用以外には使用できません。
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価格
[在庫・価格 ：2025年04月26日 17時55分現在]
※ 表示されている納期は弊社に在庫が無く、取り寄せた場合の納期目安となります。
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Anti-SP-D, Goat-Poly |
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Anti-Human SP-D Affinity Purified Polyclonal Ab |
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[在庫・価格 ：2025年04月26日 17時55分現在]
※ 表示されている納期は弊社に在庫が無く、取り寄せた場合の納期目安となります。
Anti-SP-D, Goat-Poly
文献数： 2
- 商品コード：AF1920
- メーカー：RSD
- 包装：100μg
- 価格：¥106,000
- 在庫：無(未発注)
- 納期：10日程度 ※※ 表示されている納期は弊社に在庫がなく、取り寄せた場合の目安納期となります。
- 法規制等：
| 説明文 | 別名：COLEC7collectin-7 Genbank No： 6441 Protein Accession No： P35247 |
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| 別包装品 | 別包装品あり | ||||||
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| 保存条件 | -20℃ | 法規備考 | |||||
| 抗原種 | Human | 免疫動物 | Goat | ||||
| 交差性 | Human | 適用 | Simple Western,Western Blot | ||||
| 標識 | Unlabeled | 性状 | Antigen Affinity Purified | ||||
| 吸収処理 | クラス | IgG | |||||
| クロナリティ | Polyclonal | フォーマット | |||||
| 掲載カタログ |
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| 製品記事 | Quantikine Human / Mouse SP-D ELISA Kit |
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Anti-Human SP-D Affinity Purified Polyclonal Ab
文献数： 0
- 商品コード：AF1920-SP
- メーカー：RSD
- 包装：25μg
- 価格：¥30,000
- 在庫：無(未発注)
- 納期：2～3週間 ※※ 表示されている納期は弊社に在庫がなく、取り寄せた場合の目安納期となります。
- 法規制等：
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Product Details
| Species Reactivity | Human, Mouse, Rat |
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| Label | Unconjugated |
| Immunogen | Mouse myeloma cell line NS0-derived recombinant human SP-DAla21-Phe375 (Glu22Gly)Accession # P35247 |
| Source | Polyclonal Goat IgG |
| Purification | Antigen Affinity-purified |
| Specificity | Detects human SP-D in direct ELISAs and human, mouse, and rat SP-D in Western blots. |
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Applications and Data
| Recommended Concentration | Sample | |
| Western Blot | 0.2 µg/mL | See below |
| Simple Western | 10 µg/mL | See below |
| Western Blot | |
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 | Detection of Human, Mouse, and RatSP‑D by Western Blot. Western blot shows lysates of human lung tissue, mouse lung tissue, and rat lung tissue. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Human/Mouse/Rat SP‑D Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1920) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for SP‑D at approximately 43 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1. |
| Simple Western | |
 | Detection of Human and Mouse SP‑D by Simple WesternTM. Simple Western lane view shows lysates of human lung tissue and mouse lung tissue, loaded at 0.2 mg/mL. A specific band was detected for SP‑D at approximately 64/59 kDa (as indicated) using 10 µg/mL of Goat Anti-Human/Mouse/Rat SP‑D Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1920) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody. |
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Related Product & Information
| Background | SP-D |
|---|---|
| background_content | Background: SP-D SP-D (surfactant protein-D; also PSP-D) is a 43 kDa member of the collectin family of innate immune modulators. It is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures. Its principal components consist of a collagen-like region and a C-terminal carbohydrate recognition domain (CRD), a structure that further places it in a subset of an expanded group of proteins termed defense collagens (1‑4). Human SP-D is synthesized as a 375 amino acid (aa) precursor. It contains a 20 aa signal sequence and a 355 aa mature region. The mature molecule is characterized by the presence of a 25 aa N-terminal linking-region, a 177 aa hydroxyproline and hydroxylysine collagen-like domain, a 46 aa coiled-coil segment, and a 106 aa, C-terminal collectin-like C-type lectin domain (CRD) (5, 6). Two additional, potential isoforms exist. One shows a 13 aa N-terminal extension, while the other combines the N-terminal extension with a deletion of aa’s 206‑375. Mature human SP-D shares 75% and 78% aa identity with mouse and pig SP-D, respectively. Monomeric SP-D is unusual (3). The basic form of SP-D is that of a glycosylated, disulfide-linked 150 kDa trimer that generates an alpha -helical coiled-coil structure linked to a “head” of three symmetrical CRDs (4, 7). Each CRD recognizes the hydroxides of one monosaccharide (4). Trimerization allows for the discrimination of monosaccharide patterns specific to microbial pathogens (7). Typically, SP-D forms a higher-order 620 kDa, X-shaped dodecamer through disulfide bonds associated with the N-terminus (8). This allows for even finer discrimination of self vs. nonself carbohydrate patterns, and facilitates binding to complex antigens (8, 9). One polymorphism, a Met11‑Thr11 transition in human, apparently precludes the formation of oligomers, potentially affecting the ability of affected individuals to interact with microorganisms (9, 10). Finally, SP-D is known to bind both SIRP alpha and the calreticulin/CD91 complex on macrophages. When the ratio of antigen/pathogen to available CRDs is low, antigen can be bound without occupying all available CRDs. The free CRDs will bind to SIRP alpha, generating a signal that downmodulates the inflammatory response. When virtually all CRDs are occupied by ligand, however, free CRDs are not available for SIRP alpha binding. Instead, the dodecamer is depicted to undergo a structural rearrangement, exposing the N-termini of all four linked trimers. This exposed terminus is known to bind to the calreticulin/CD91 complex, an event that initiates inflammation. Thus, it would appear that SP-D allows for a graded response to environmental challenge. SP-D provides a mechanism for the clearance of small antigenic insults without the need for a damaging inflammatory response (3). |
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Citations
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
- Oxidative damage of SP-D abolishes control of eosinophil extracellular DNA trap formation
Authors: S Yousefi, SK Sharma, D Stojkov, N Germic, S Aeschliman, MQ Ge, CH Flayer, ED Larson, IG Redai, S Zhang, CJ Koziol-Whi, K Karikó, HU Simon, A Haczku
J. Leukoc. Biol., 2018;0(0):.
Species: Mouse
Sample Type: BALF
Application: WB - MMP-9 cleaves SP-D and abrogates its innate immune functions in vitro.
Authors: Bratcher, Preston, Weathington, Nathanie, Nick, Heidi J, Jackson, Patricia, Snelgrove, Robert J, Gaggar, Amit
PLoS ONE, 2012;7(7):e41881.
Species: Human
Sample Type: Recombinant Protein
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